|
Name |
Accession |
Description |
Interval |
E-value |
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
1-1292 |
0e+00 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 2330.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 1 MSQHLPLVAAQPGIWMAEKLSELPSAWSVAHYVELTGEVDSPLLARAVVAGLAQADTLRMRFTEDNGEVWQWVDDALTFE 80
Cdd:PRK10252 4 MSQHLPLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDPALTFP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 81 LPEIIDLRTNIDPHGTAQALMQADLQQDLRVDSGKPLVFHQLIQVADNRWYWYQRYHHLLVDGFSFPAITRQIANIYCTW 160
Cdd:PRK10252 84 LPEIIDLRTQPDPHAAAQALMQADLQQDLRVDSGKPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 161 LRGEPTPASPFTPFADVVEEYQQYRESEAWQRDAAFWAEQRRQLPPPASLSPAPLPGRSASADILRLKLEFTDGEFRQLA 240
Cdd:PRK10252 164 LRGEPTPASPFTPFADVVEEYQRYRASEAWQRDAAFWAEQRRQLPPPASLSPAPLPGRSASADILRLKLEFTDGAFRQLA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 241 TQLSGVQRTDLALALAALWLGRLCNRMDYAAGFIFMRRLGSAALTATGPVLNVLPLGIHIAAQETLPELATRLAAQLKKM 320
Cdd:PRK10252 244 AQASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQETLPELATRLAAQLKKM 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 321 RRHQRYDAEQIVRDSGRAAGDEPLFGPVLNIKVFDYQLDIPDVQAQTHTLATGPVNDLELALFPDVHGDLSIEILANKQR 400
Cdd:PRK10252 324 RRHQRYDAEQIVRDSGRAAGDEPLFGPVLNIKVFDYQLDFPGVQAQTHTLATGPVNDLELALFPDEHGGLSIEILANPQR 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 401 YDEPTLIQHAERLKMLIAQFAADPALLCGDVDIMLPGEYAQLAQLNATQVEIPETTLSALVAEQAAKTPDAPALADARYL 480
Cdd:PRK10252 404 YDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEYAQLAQVNATAVEIPETTLSALVAQQAAKTPDAPALADARYQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 481 FSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTD 560
Cdd:PRK10252 484 FSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTA 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 561 DQLPRFSDVPNLTSLCYNAPLTPQGSAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTGEDVVA 640
Cdd:PRK10252 564 DQLPRFADVPDLTSLCYNAPLAPQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVL 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 641 QKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPQTARQSCATLKQVF 720
Cdd:PRK10252 644 QKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPEGARQSCASLRQVF 723
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 721 CSGEALPADLCREWQQLTGAPLHNLYGPTEAAVDVSWYPAFGEELAQVRGSSVPIGYPVWNTGLRILDAMMHPVPPGVAG 800
Cdd:PRK10252 724 CSGEALPADLCREWQQLTGAPLHNLYGPTEAAVDVSWYPAFGEELAAVRGSSVPIGYPVWNTGLRILDARMRPVPPGVAG 803
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 801 DLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALP 880
Cdd:PRK10252 804 DLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALP 883
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 881 DVEQAVTHACVINQAAATGGDARQLVGYLVSQSGLPLDTSALQAQLRETLPPHMVPVVLLQLPQLPLSANGKLDRKALPL 960
Cdd:PRK10252 884 DVEQAVTHACVINQAAATGGDARQLVGYLVSQSGLPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKALPL 963
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 961 PELKAQAPGRAPKAGSETIIAAAFSSLLGCDVQDADADFFALGGHSLLAMKLAAQLSRQVARQVTPGQVMVASTVAKLAT 1040
Cdd:PRK10252 964 PELKAQVPGRAPKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKLAT 1043
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 1041 IIDAEEDSTRRMGFETILPLREGNGPTLFCFHPASGFAWQFSVLSRYLDPQWSIIGIQSPRPNGPMQTAANLDEVCEAHL 1120
Cdd:PRK10252 1044 LLDAEEDESRRLGFGTILPLREGDGPTLFCFHPASGFAWQFSVLSRYLDPQWSIYGIQSPRPDGPMQTATSLDEVCEAHL 1123
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 1121 ATLLEQQPHGPYYLLGYSLGGTLAQGIAARLRARGEQVAFLGLLDTWPPETQNWQEKEANGLDPEVLAEINREREAFLAA 1200
Cdd:PRK10252 1124 ATLLEQQPHGPYHLLGYSLGGTLAQGIAARLRARGEEVAFLGLLDTWPPETQNWREKEANGLDPEVLAEIDREREAFLAA 1203
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 1201 QQGSTSTELFTTIEGNYADAVRLLTTAHSVPFDGKATLFVAERTLQEGMSPERAWSPWIAELDIYRQDCAHVDIISPGTF 1280
Cdd:PRK10252 1204 QQGSLSTELFTTIEGNYADAVRLLTTAHSVPFDGKATLFVAERTLQEGMSPEQAWSPWIAELDVYRQDCAHVDIISPEAF 1283
|
1290
....*....|..
gi 16128569 1281 EKIGPIIRATLN 1292
Cdd:PRK10252 1284 EKIGPILRATLN 1295
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1-1165 |
0e+00 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 734.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 1 MSQHLPLVAAQPGIWMAEKLSELPSAWSVAHYVELTGEVDSPLLARAVVAGLAQADTLRMRFTEDNGEVWQWVDDALTFE 80
Cdd:COG1020 14 AAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPVVAAP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 81 LPEIIDLRTNIDPHGTAQALMQADLQQDLRVDSGKPLVFHQLIQVADNRWYWYQRYHHLLVDGFSFPAITRQIANIYCTW 160
Cdd:COG1020 94 LPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLAA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 161 LRGEPTP-ASPFTPFADVVEEYQQYRESEAWQRDAAFWAEQRRQLPPPASLSPAPLPGRSASADILRLKLEFTDGEFRQL 239
Cdd:COG1020 174 YAGAPLPlPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFRLPAELTAAL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 240 aTQLSGVQRTDLALALAALW---LGRLCNRMDYAAGFIFMRRLGSAALTATGPVLNVLPLGIHIAAQETLPELATRLAAQ 316
Cdd:COG1020 254 -RALARRHGVTLFMVLLAAFallLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRET 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 317 LKKMRRHQRYDAEQIVRDSG--RAAGDEPLFGPVLNIKVFDY-QLDIPDVQAQTHTLATGPVN-DLELALFPDvHGDLSI 392
Cdd:COG1020 333 LLAAYAHQDLPFERLVEELQpeRDLSRNPLFQVMFVLQNAPAdELELPGLTLEPLELDSGTAKfDLTLTVVET-GDGLRL 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 393 EILANKQRYDEPTLIQHAERLKMLIAQFAADPALLCGDVDIMLPGEYAQ-LAQLNATQVEIP-ETTLSALVAEQAAKTPD 470
Cdd:COG1020 412 TLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQlLAEWNATAAPYPaDATLHELFEAQAARTPD 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 471 APALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLED 550
Cdd:COG1020 492 AVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLED 571
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 551 ARPSLLITTDDQLPRFSDvPNLTSLCYNAPLTPQGSA--PLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQ 628
Cdd:COG1020 572 AGARLVLTQSALAARLPE-LGVPVLALDALALAAEPAtnPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQ 650
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 629 NHYPLTGEDVVAQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASltpqt 708
Cdd:COG1020 651 RRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLDA----- 725
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 709 ARQSCATLKQVFCSGEALPADLCREWQQ-LTGAPLHNLYGPTEAAVDVSWYPAFGEELAqvrGSSVPIGYPVWNTGLRIL 787
Cdd:COG1020 726 APEALPSLRLVLVGGEALPPELVRRWRArLPGARLVNLYGPTETTVDSTYYEVTPPDAD---GGSVPIGRPIANTRVYVL 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 788 DAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPF-APGERMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQR 866
Cdd:COG1020 803 DAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFgFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFR 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 867 IELGEIDRVMQALPDVEQAVthacVInqAAATGGDARQLVGYLVSQSGLPLDTSALQAQLRETLPPHMVPVVLLQLPQLP 946
Cdd:COG1020 883 IELGEIEAALLQHPGVREAV----VV--AREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLP 956
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 947 LSANGKLDRKALPLPELKAQAPGRAPKAGSETIIAAAFSSLLGCDVQDADADFFALGGHSLLAMKLAAQLSRQVARQVTP 1026
Cdd:COG1020 957 LTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLL 1036
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 1027 GQVMVASTVAKLATIIDAEEDSTRRmgfETILPLREGNGPTLFCFHPASGFAWQFSVLSRYLDPQWSIIGIQSPRPNGPM 1106
Cdd:COG1020 1037 LLLFLAAAAAAAAAAAAAAAAAAAA---PLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLL 1113
|
1130 1140 1150 1160 1170
....*....|....*....|....*....|....*....|....*....|....*....
gi 16128569 1107 QTAANLDEVCEAHLATLLEQQPHGPYYLLGYSLGGTLAQGIAARLRARGEQVAFLGLLD 1165
Cdd:COG1020 1114 LLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAA 1172
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
459-958 |
0e+00 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 707.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 459 ALVAEQAAKTPDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTG 538
Cdd:cd17646 2 ALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 539 YPDDRLKMMLEDARPSLLITTDDQLPRFSDVPNLTSLCYNAPLTPQGSAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQT 618
Cdd:cd17646 82 YPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 619 AIVNRLLWMQNHYPLTGEDVVAQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLA 698
Cdd:cd17646 162 GIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVPSMLR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 699 AFVASLTPqtarQSCATLKQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVDVSWYPAFGEElaqvRGSSVPIGYP 778
Cdd:cd17646 242 VFLAEPAA----GSCASLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVTHWPVRGPA----ETPSVPIGRP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 779 VWNTGLRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDNGAVEYLGRSDD 858
Cdd:cd17646 314 VPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDD 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 859 QLKIRGQRIELGEIDRVMQALPdveqAVTHACVINQAAATGGdaRQLVGYLVSQSG-LPLDTSALQAQLRETLPPHMVPV 937
Cdd:cd17646 394 QVKIRGFRVEPGEIEAALAAHP----AVTHAVVVARAAPAGA--ARLVGYVVPAAGaAGPDTAALRAHLAERLPEYMVPA 467
|
490 500
....*....|....*....|.
gi 16128569 938 VLLQLPQLPLSANGKLDRKAL 958
Cdd:cd17646 468 AFVVLDALPLTANGKLDRAAL 488
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
469-958 |
0e+00 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 577.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 469 PDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMML 548
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 549 EDARPSLLITTDDQLprfsdvpnltslcynapltpqgsaplqlsqphhtAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQ 628
Cdd:cd05930 81 EDSGAKLVLTDPDDL----------------------------------AYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 629 NHYPLTGEDVVAQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPQT 708
Cdd:cd05930 127 EAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELAA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 709 arqsCATLKQVFCSGEALPADLCREWQQL-TGAPLHNLYGPTEAAVDVSWYPAFGEELAqvrGSSVPIGYPVWNTGLRIL 787
Cdd:cd05930 207 ----LPSLRLVLVGGEALPPDLVRRWRELlPGARLVNLYGPTEATVDATYYRVPPDDEE---DGRVPIGRPIPNTRVYVL 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 788 DAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRI 867
Cdd:cd05930 280 DENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRI 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 868 ELGEIDRVMQALPDVEQAVthacVINQAAATGGDarQLVGYLVSQSGLPLDTSALQAQLRETLPPHMVPVVLLQLPQLPL 947
Cdd:cd05930 360 ELGEIEAALLAHPGVREAA----VVAREDGDGEK--RLVAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPL 433
|
490
....*....|.
gi 16128569 948 SANGKLDRKAL 958
Cdd:cd05930 434 TPNGKVDRKAL 444
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
4-424 |
2.16e-170 |
|
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380456 [Multi-domain] Cd Length: 419 Bit Score: 512.30 E-value: 2.16e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 4 HLPLVAAQPGIWMAEKLSELPSAWSVAHYVELTGEVDSPLLARAVVAGLAQADTLRMRFTEDNGEVWQWVDDaLTFELPE 83
Cdd:cd19533 1 RLPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDP-YTPVPIR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 84 IIDLRTNIDPHGTAQALMQADLQQDLrVDSGKPLVFHQLIQVADNRWYWYQRYHHLLVDGFSFPAITRQIANIYCTWLRG 163
Cdd:cd19533 80 HIDLSGDPDPEGAAQQWMQEDLRKPL-PLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALLKG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 164 EPTPASPFTPFADVVEEYQQYRESEAWQRDAAFWAEQRRQLPPPASLSPAplpGRSASADILRLKLEFTDGEFRQLATQL 243
Cdd:cd19533 159 RPAPPAPFGSFLDLVEEEQAYRQSERFERDRAFWTEQFEDLPEPVSLARR---APGRSLAFLRRTAELPPELTRTLLEAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 244 S--GVQRTDLALALAALWLGRLCNRMDYAAGFIFMRRLGSAALTATGPVLNVLPLGIHIAAQETLPELATRLAAQLKKMR 321
Cdd:cd19533 236 EahGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPQQTFAELVAQVSRELRSLL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 322 RHQRYDAEQIVRDSGRAAGDEPLFGPVLNIKVFDYQLDIPDVQAQTHTLATGPVNDLELALFP-DVHGDLSIEILANKQR 400
Cdd:cd19533 316 RHQRYRYEDLRRDLGLTGELHPLFGPTVNYMPFDYGLDFGGVVGLTHNLSSGPTNDLSIFVYDrDDESGLRIDFDANPAL 395
|
410 420
....*....|....*....|....
gi 16128569 401 YDEPTLIQHAERLKMLIAQFAADP 424
Cdd:cd19533 396 YSGEDLARHQERLLRLLEEAAADP 419
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
85-1169 |
4.06e-165 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 548.22 E-value: 4.06e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 85 IDLRTNIDPHGTAQALMQADLQQDLRVDSGkPLVFHQLIQVADNRWYWYQRYHHLLVDGFSFPAITRQIANIYctwlRGE 164
Cdd:PRK12467 2727 LDWRDRADLEQALDALAAADRQQGFDLLSA-PLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLLGEVLQRY----FGQ 2801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 165 PTPASPftpfadvveeyQQYRESEAW------QRDAAFWAEQ----RRQLPPPASLSPAPLPGRSASADIlRLKLEFTdg 234
Cdd:PRK12467 2802 PPPARE-----------GRYRDYIAWlqaqdaEASEAFWKEQlaalEEPTRLARALYPAPAEAVAGHGAH-YLHLDAT-- 2867
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 235 EFRQLAtQLSGVQRTDLALALAALW---LGRLCNRMDYAAGFIFMRRLGS--AALTATGPVLNVLPLGIHIAAQETLPEL 309
Cdd:PRK12467 2868 QTRQLI-EFARRHRVTLNTLVQGAWlllLQRFTGQDTVCFGATVAGRPAQlrGAEQQLGLFINTLPVIASPRAEQTVSDW 2946
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 310 ATRLAAQLKKMRRHQRYDAEQIVRDSGRaaGDEPLFGpvlNIKVFD-YQLDIPDVQAQTHTLATGPVNDLELALFP---D 385
Cdd:PRK12467 2947 LQQVQAQNLALREFEHTPLADIQRWAGQ--GGEALFD---SILVFEnYPISEALKQGAPSGLRFGAVSSREQTNYPltlA 3021
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 386 VH-GD-LSIEILANKQRYDEPTLIQHAERLKMLIAQFAADPALLCGDVDIMLPGEYAQLAQ-LNATQVEIP-ETTLSALV 461
Cdd:PRK12467 3022 VGlGDtLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHaWNATAAAYPsERLVHQLI 3101
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 462 AEQAAKTPDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPD 541
Cdd:PRK12467 3102 EAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPR 3181
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 542 DRLKMMLEDARPSLLITTD---DQLPRFSDVPNLT----SLCYNAPLTPQGSAplqlsQPHHTAYIIFTSGSTGRPKGVM 614
Cdd:PRK12467 3182 ERLAYMIEDSGVKLLLTQAhllEQLPAPAGDTALTldrlDLNGYSENNPSTRV-----MGENLAYVIYTSGSTGKPKGVG 3256
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 615 VGQTAIVNRLLWMQNHYPLTGEDVVAQKTPCSFDVSVWEFFWPFIAGAKLVMAePEAHRDPLAMQQFFAEYGVTTTHFVP 694
Cdd:PRK12467 3257 VRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVR-DNDLWDPEELWQAIHAHRISIACFPP 3335
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 695 SMLAAFVASltpqTARQSCATLKQVFCSGEALPAD-LCREWQQLTGAPLHNLYGPTEAAVDVSWYPAFGEelAQVRGSSV 773
Cdd:PRK12467 3336 AYLQQFAED----AGGADCASLDIYVFGGEAVPPAaFEQVKRKLKPRGLTNGYGPTEAVVTVTLWKCGGD--AVCEAPYA 3409
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 774 PIGYPVWNTGLRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAP-GERMYRTGDVARWLDNGAVEY 852
Cdd:PRK12467 3410 PIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSGsGGRLYRTGDLARYRADGVIEY 3489
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 853 LGRSDDQLKIRGQRIELGEIDRVMQALPDVEQAVthacVINQAAATGgdaRQLVGYLVSQSGLPLDTSALQAQLRETLPP 932
Cdd:PRK12467 3490 LGRIDHQVKIRGFRIELGEIEARLLQHPSVREAV----VLARDGAGG---KQLVAYVVPADPQGDWRETLRDHLAASLPD 3562
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 933 HMVPVVLLQLPQLPLSANGKLDRKALPLPELKAQAPGRAPKAGSETIIAAAFSSLLGCDVQDADADFFALGGHSLLAMKL 1012
Cdd:PRK12467 3563 YMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKGSREYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQV 3642
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 1013 AAQLSRQVARQVTPGQVMVASTVAKLATIIDAEEdstrrMGFETILPL--REGNGPTLFCFHPASGFAWQFSVLSRYLDP 1090
Cdd:PRK12467 3643 LSRIRQSLGLKLSLRDLMSAPTIAELAGYSPLGD-----VPVNLLLDLnrLETGFPALFCRHEGLGTVFDYEPLAVILEG 3717
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128569 1091 QWSIIGIQSPRPNGPMQTAANLDEVCEAHLATLLEQQPHGPYYLLGYSLGGTLAQGIAARLRARGEQVAFLGLLDTWPP 1169
Cdd:PRK12467 3718 DRHVLGLTCRHLLDDGWQDTSLQAMAVQYADYILWQQAKGPYGLLGWSLGGTLARLVAELLEREGESEAFLGLFDNTLP 3796
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
3-1041 |
3.28e-157 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 524.73 E-value: 3.28e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 3 QHLPLVAAQPGIWMAEKLSELPSAWSVAHYVELTGEVDSPLLARAVVAGLAQADTLRMRFTEDNGEVWQWVDDA--LTFE 80
Cdd:PRK12467 1115 QPLPLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVIHPVgsLTLE 1194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 81 LPEiidLRTNIDPHGTAQALMQADLQQDLRVDSGkPLVFHQLIQVADNRWYWYQRYHHLLVDGFSFPAITRQIANIYCTW 160
Cdd:PRK12467 1195 EPL---LLAADKDEAQLKVYVEAEARQPFDLEQG-PLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAY 1270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 161 LRGEpTPASPFTP--FADVVEEYQQYRESEAWQRDAAFWAEQ--RRQLPPPASLSPAPLPGRSASADILRLKL--EFTDG 234
Cdd:PRK12467 1271 SQGQ-SLQLPALPiqYADYAVWQRQWMDAGERARQLAYWKAQlgGEQPVLELPTDRPRPAVQSHRGARLAFELppALAEG 1349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 235 eFRQLAtQLSGVQRTDLALALAALWLGRLCNRMDYAAGFIFMRRLGSAALTATGPVLNVLPLGIHIAAQETLPEL----- 309
Cdd:PRK12467 1350 -LRALA-RREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASFQQLlqqvk 1427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 310 ATRLAAQLkkmrrHQRYDAEQIVR--DSGRAAGDEPLFGpvlniKVFDYQLDIPDVQAQTHTLATGPVN--------DLE 379
Cdd:PRK12467 1428 QAALEAQA-----HQDLPFEQLVEalQPERSLSHSPLFQ-----VMFNHQRDDHQAQAQLPGLSVESLSwesqtaqfDLT 1497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 380 LALFPDVHGdLSIEILANKQRYDEPTLIQHAERLKMLIAQFAADPALLCGDVDIMLPGEYAQLAQL-NATQVEIP-ETTL 457
Cdd:PRK12467 1498 LDTYESSEG-LQASLTYATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEGwNATHTGYPlARLV 1576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 458 SALVAEQAAKTPDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDT 537
Cdd:PRK12467 1577 HQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDP 1656
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 538 GYPDDRLKMMLEDARPSLLITTDDQLPRFSDVPNLTSLCYNAP---LTPQG-SAPLQLSQPHHTAYIIFTSGSTGRPKGV 613
Cdd:PRK12467 1657 EYPRERLAYMIEDSGIELLLTQSHLQARLPLPDGLRSLVLDQEddwLEGYSdSNPAVNLAPQNLAYVIYTSGSTGRPKGA 1736
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 614 MVGQTAIVNRLLWMQNHYPLTGEDVVAQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFV 693
Cdd:PRK12467 1737 GNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFV 1816
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 694 PSMLAAFVaSLTPQTARqsCATLKQVFCSGEALPADLCREW-QQLTGAPLHNLYGPTEAAVDVSWYPAFGEELAQvrGSS 772
Cdd:PRK12467 1817 PSMLQQLL-QMDEQVEH--PLSLRRVVCGGEALEVEALRPWlERLPDTGLFNLYGPTETAVDVTHWTCRRKDLEG--RDS 1891
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 773 VPIGYPVWNTGLRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFA-PGERMYRTGDVARWLDNGAVE 851
Cdd:PRK12467 1892 VPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFGtVGSRLYRTGDLARYRADGVIE 1971
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 852 YLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQAVTHACvinqaaaTGGDARQLVGYLVSQSGLPLDT--------SALQ 923
Cdd:PRK12467 1972 YLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQ-------DGANGKQLVAYVVPTDPGLVDDdeaqvalrAILK 2044
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 924 AQLRETLPPHMVPVVLLQLPQLPLSANGKLDRKALPLPELKA-QAPGRAPKAGSETIIAAAFSSLLGCDVQDADADFFAL 1002
Cdd:PRK12467 2045 NHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDASElQQAYVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFEL 2124
|
1050 1060 1070
....*....|....*....|....*....|....*....
gi 16128569 1003 GGHSLLAMKLAAQlSRQVARQVTPGQVMVASTVAKLATI 1041
Cdd:PRK12467 2125 GGDSIISIQVVSR-ARQAGIRFTPKDLFQHQTVQSLAAV 2162
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
5-1053 |
2.41e-156 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 522.60 E-value: 2.41e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 5 LPLVAAQPGIWMAEKLSELPSAWSVAHYVELTGEVDSPLLARAVVAGLAQADTLRMRFTEDNGEVWQWVDDALTFELpEI 84
Cdd:PRK12316 50 DRLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQVPLDRPLEV-EF 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 85 IDLRtnidphGTAQALMQADLQQDLRVDSGKP-------LVFHQLIQVADNRWYWYQRYHHLLVDGFSFPAITRQIANIY 157
Cdd:PRK12316 129 EDCS------GLPEAEQEARLRDEAQRESLQPfdlcegpLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFY 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 158 CTWLRGEpTPASPFTPFadvveeyqQYRESEAWQRDAAFWAEQRRQLPPPASLSPAPL--------PGRSASADILRLKL 229
Cdd:PRK12316 203 SAYATGA-EPGLPALPI--------QYADYALWQRSWLEAGEQERQLEYWRAQLGEEHpvlelptdHPRPAVPSYRGSRY 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 230 EFTDGEfrQLATQLSGVQRTdlalalaalwlGRLCNRMDYAAGF--IFMRRLGSAALTATGPVLN--------VLPLGIH 299
Cdd:PRK12316 274 EFSIDP--ALAEALRGTARR-----------QGLTLFMLLLGAFnvLLHRYSGQTDIRVGVPIANrnraevegLIGFFVN 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 300 IAAQETLPELATRLAAQLKKMRR-------HQRYDAEQIVR--DSGRAAGDEPLFGPVLNikvfdYQLDIPDVQAQTHtl 370
Cdd:PRK12316 341 TQVLRSVFDGRTRVATLLAGVKDtvlgaqaHQDLPFERLVEalKVERSLSHSPLFQVMYN-----HQPLVADIEALDT-- 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 371 atgpVNDLELALFP----DVHGDLSIEILANKQR-----------YDEPTLIQHAERLKMLIAQFAADPALLCGDVDIML 435
Cdd:PRK12316 414 ----VAGLEFGQLEwksrTTQFDLTLDTYEKGGRlhaaltyatdlFEARTVERMARHWQNLLRGMVENPQARVDELPMLD 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 436 PGEYAQLAQ-LNATQVEIP-ETTLSALVAEQAAKTPDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALP 513
Cdd:PRK12316 490 AEERGQLVEgWNATAAEYPlQRGVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAME 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 514 RSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITtDDQLPRFSDVPN-LTSLCYNAP---LTPQGSAPL 589
Cdd:PRK12316 570 RSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLS-QSHLGRKLPLAAgVQVLDLDRPaawLEGYSEENP 648
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 590 QLS-QPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTGEDVVAQKTPCSFDVSVWEFFWPFIAGAKLVMAE 668
Cdd:PRK12316 649 GTElNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAA 728
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 669 PEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVasltPQTARQSCATLKQVFCSGEALPADLCRE-WQQLTGAPLHNLYG 747
Cdd:PRK12316 729 PGDHRDPAKLVELINREGVDTLHFVPSMLQAFL----QDEDVASCTSLRRIVCSGEALPADAQEQvFAKLPQAGLYNLYG 804
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 748 PTEAAVDVSWYPAFGEElaqvrGSSVPIGYPVWNTGLRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIAD 827
Cdd:PRK12316 805 PTEAAIDVTHWTCVEEG-----GDSVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPS 879
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 828 PFAPGERMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQAVTHACvinqaaatggDARQLVG 907
Cdd:PRK12316 880 PFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV----------DGKQLVG 949
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 908 YLVSQSGLPLDTSALQAQLRETLPPHMVPVVLLQLPQLPLSANGKLDRKALPLPEL-KAQAPGRAPKAGSETIIAAAFSS 986
Cdd:PRK12316 950 YVVLESEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEAsVAQQGYVAPRNALERTLAAIWQD 1029
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128569 987 LLGCDVQDADADFFALGGHSLLAMKLAAQlSRQVARQVTPGQVMVASTVAKLATIIDAEEDSTRRMG 1053
Cdd:PRK12316 1030 VLGVERVGLDDNFFELGGDSIVSIQVVSR-ARQAGIQLSPRDLFQHQTIRSLALVAKAGQATAADQG 1095
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
3-1057 |
4.68e-156 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 521.65 E-value: 4.68e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 3 QHLPLVAAQPGIWMAEKLSELPSAWSVAHYVELTGEVDSPLLARAVVAGLAQADTLRMRFTEDNGEVWQWVDDALTFELp 82
Cdd:PRK05691 674 QALPQSLAQNRLWLLWQLDPQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYERDGVALQRIDAQGEFAL- 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 83 EIIDLRTNIDPHGTAQALMQADLQQDLRVDSGK-PLVFHQLIQVADNRWYWYQRYHHLLVDGFSFPAITRQIANIYCTWL 161
Cdd:PRK05691 753 QRIDLSDLPEAEREARAAQIREEEARQPFDLEKgPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAAC 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 162 RGEPTPASPFT-PFADVVEEYQQYRESEAWQRDAAFWAEQRRQLPPPASLSPAPLPG----RSASADILRLKLEFTDGeF 236
Cdd:PRK05691 833 QGQTAELAPLPlGYADYGAWQRQWLAQGEAARQLAYWKAQLGDEQPVLELATDHPRSarqaHSAARYSLRVDASLSEA-L 911
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 237 RQLATQlsgvQRTDLALALAALW---LGRLCNRMDYAAGFIFMRRLGSAALTATGPVLNVLPLGIHIAAQETLPEL---- 309
Cdd:PRK05691 912 RGLAQA----HQATLFMVLLAAFqalLHRYSGQGDIRIGVPNANRPRLETQGLVGFFINTQVLRAQLDGRLPFTALlaqv 987
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 310 -ATRLAAQlkkmrRHQRYDAEQIVRDSGRAaGDEPLFGPVLNIKvfdyQLDIPDVQAQTHTLATG-PVN------DLELA 381
Cdd:PRK05691 988 rQATLGAQ-----AHQDLPFEQLVEALPQA-REQGLFQVMFNHQ----QRDLSALRRLPGLLAEElPWHsreakfDLQLH 1057
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 382 LFPDVHGDLSIEILANKQRYDEPTLIQHAERLKMLIAQFAADPALLCGDVDIMLPGEYAQLAQLNATQVEIPETTLSALV 461
Cdd:PRK05691 1058 SEEDRNGRLTLSFDYAAELFDAATIERLAEHFLALLEQVCEDPQRALGDVQLLDAAERAQLAQWGQAPCAPAQAWLPELL 1137
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 462 AEQAAKTPDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPD 541
Cdd:PRK05691 1138 NEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPA 1217
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 542 DRLKMMLEDARPSLLITTDDQLPRFSDVPNLTSLCY------NAPLTPQGsapLQLSQpHHTAYIIFTSGSTGRPKGVMV 615
Cdd:PRK05691 1218 ERLAYMLADSGVELLLTQSHLLERLPQAEGVSAIALdslhldSWPSQAPG---LHLHG-DNLAYVIYTSGSTGQPKGVGN 1293
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 616 GQTAIVNRLLWMQNHYPLTGEDVVAQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPS 695
Cdd:PRK05691 1294 THAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVPP 1373
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 696 MLAAFVAsltpQTARQSCATLKQVFCSGEALPADLC-REWQQLTGAPLHNLYGPTEAAVDVSWYPAFGEElaqvrGSSVP 774
Cdd:PRK05691 1374 LLQLFID----EPLAAACTSLRRLFSGGEALPAELRnRVLQRLPQVQLHNRYGPTETAINVTHWQCQAED-----GERSP 1444
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 775 IGYPVWNTGLRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFA-PGERMYRTGDVARWLDNGAVEYL 853
Cdd:PRK05691 1445 IGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLGeDGARLYRTGDRARWNADGALEYL 1524
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 854 GRSDDQLKIRGQRIELGEIDRVMQALPDVEQAVThacVINQAAAtggdARQLVGYLVSQSGLPLDTSALQAQLRETLPPH 933
Cdd:PRK05691 1525 GRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAV---LVREGAA----GAQLVGYYTGEAGQEAEAERLKAALAAELPEY 1597
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 934 MVPVVLLQLPQLPLSANGKLDRKALPLPELKaQAPGRAPKAGSETIIAAAFSSLLGCDVQDADADFFALGGHSLLAMKLA 1013
Cdd:PRK05691 1598 MVPAQLIRLDQMPLGPSGKLDRRALPEPVWQ-QREHVEPRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIV 1676
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....*
gi 16128569 1014 AQlSRQVARQVTPGQVMV-ASTVAKLATIIDAEEDSTRRMGFETI 1057
Cdd:PRK05691 1677 SR-TRQACDVELPLRALFeASELGAFAEQVARIQAAGERNSQGAI 1720
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
3-1049 |
4.75e-156 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 521.26 E-value: 4.75e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 3 QHLPLVAAQPGIWMAEKLSELPSAWSVAHYVELTGEVDSPLLARAVVAGLAQADTLRMRFTEDNGEVWQWVDDALTFELP 82
Cdd:PRK12467 48 ERIPLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEEGFRQVIDASLSLTIP 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 83 -EIIDLRTNIDPHGTAQALMQADLQQDLRVDSGkPLVFHQLIQVADNRWYWYQRYHHLLVDGFSFPAITRQIANIYCTWL 161
Cdd:PRK12467 128 lDDLANEQGRARESQIEAYINEEVARPFDLANG-PLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYS 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 162 RG-EPT-PASPFtpfadvveeyqQYRESEAWQR---DA-------AFWAEQ--RRQLPPPASLSPAPLPGRSASADILRL 227
Cdd:PRK12467 207 QGrEPSlPALPI-----------QYADYAIWQRswlEAgererqlAYWQEQlgGEHTVLELPTDRPRPAVPSYRGARLRV 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 228 KLEftdgefRQLATQLSGVQRTD------LALALAALWLGRLCNRMDYAAGFIFMRRLGSAALTATGPVLNVLPLGIHIA 301
Cdd:PRK12467 276 DLP------QALSAGLKALAQREgvtlfmVLLASFQTLLHRYSGQSDIRIGVPNANRNRVETERLIGFFVNTQVLKAEVD 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 302 AQETLPELATRLAAQLKKMRRHQRYDAEQIVR--DSGRAAGDEPLFGPVLN-------IKVFDYQ----LDIPDVQAQTH 368
Cdd:PRK12467 350 PQASFLELLQQVKRTALGAQAHQDLPFEQLVEalQPERSLSHSPLFQVMFNhqntatgGRDREGAqlpgLTVEELSWARH 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 369 TlatgpvNDLELAL-FPDVHGDLSIEILANKQRYDEPTLIQHAERLKMLIAQFAADPALLCGDVDIMLPGEYA-QLAQLN 446
Cdd:PRK12467 430 T------AQFDLALdTYESAQGLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPLLDAEERArELVRWN 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 447 ATQVEIPETTLSALVAEQAAKTPDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIV 526
Cdd:PRK12467 504 APATEYAPDCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVL 583
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 527 EAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTDDQLPRFsDVP-NLTSLCYNAPLTP-QGSAPLQLS---QPHHTAYII 601
Cdd:PRK12467 584 KAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQL-PVPaGLRSLCLDEPADLlCGYSGHNPEvalDPDNLAYVI 662
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 602 FTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTGEDVVAQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQF 681
Cdd:PRK12467 663 YTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAAL 742
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 682 FAEYGVTTTHFVPSMLAAFVasltpQTARQS-CATLKQVFCSGEALPADLCREWQQLT-GAPLHNLYGPTEAAVDVSWYP 759
Cdd:PRK12467 743 MADQGVTVLKIVPSHLQALL-----QASRVAlPRPQRALVCGGEALQVDLLARVRALGpGARLINHYGPTETTVGVSTYE 817
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 760 AFGEELAQvrgSSVPIGYPVWNTGLRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAP-GERMYRT 838
Cdd:PRK12467 818 LSDEERDF---GNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFGAdGGRLYRT 894
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 839 GDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQAVThacvinqAAATGGDARQLVGYLVSQSGLPLD 918
Cdd:PRK12467 895 GDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVV-------LAQPGDAGLQLVAYLVPAAVADGA 967
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 919 T-----SALQAQLRETLPPHMVPVVLLQLPQLPLSANGKLDRKALPLPELKA-QAPGRAPKAGSETIIAAAFSSLLGCDV 992
Cdd:PRK12467 968 EhqatrDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAvQATFVAPQTELEKRLAAIWADVLKVER 1047
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|....*..
gi 16128569 993 QDADADFFALGGHSLLAMKLAAQLSRQVARQVTPGQVMVASTVAKLATIIDAEEDST 1049
Cdd:PRK12467 1048 VGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAVAAQQQGA 1104
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
4-424 |
1.70e-150 |
|
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380453 [Multi-domain] Cd Length: 427 Bit Score: 460.72 E-value: 1.70e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 4 HLPLVAAQPGIWMAEKLSELPSAWSVAHYVELTGEVDSPLLARAVVAGLAQADTLRMRFTEDNGEVWQWVDDALTFELPE 83
Cdd:cd19066 1 KIPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVLDKTVRFRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 84 IIDLRTNIDPHGTAQALMQADLQQDlRVDSGKPLVFHQLIQVADNRWYWYQRYHHLLVDGFSFPAITRQIANIYCTWLRG 163
Cdd:cd19066 81 IIDLRNLADPEARLLELIDQIQQTI-YDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAERQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 164 EPTPASPFTPFADVVEEYQQYRESEAWQRDAAFWAEQRRQLPPPASLSPAPLPGRSASADILRLKLEFTDGEFRQL--AT 241
Cdd:cd19066 160 KPTLPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKRLreVA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 242 QLSGVQRTDLALALAALWLGRLCNRMDYAAGFIFMRRLGSAALTATGPVLNVLPLGIHIAAQETLPELATRLAAQLKKMR 321
Cdd:cd19066 240 RESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSREAI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 322 RHQRYDAEQIVRDSG--RAAGDEPLFGPVLNIKVFDYQLDIPDVQA---QTHTLATGPVNDLELALFPDVHGDLSIEILA 396
Cdd:cd19066 320 EHQRVPFIELVRHLGvvPEAPKHPLFEPVFTFKNNQQQLGKTGGFIfttPVYTSSEGTVFDLDLEASEDPDGDLLLRLEY 399
|
410 420
....*....|....*....|....*...
gi 16128569 397 NKQRYDEPTLIQHAERLKMLIAQFAADP 424
Cdd:cd19066 400 SRGVYDERTIDRFAERYMTALRQLIENP 427
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
3-1041 |
3.76e-149 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 501.02 E-value: 3.76e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 3 QHLPLVAAQPGIWMAEKLSELPSAWSVAHYVELTGEVDSPLLARAVVAGLAQADTLRMRFTEDNGEVWQWVDDALTFElp 82
Cdd:PRK12316 2601 QPLPLSHAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGEQTRQVILPNMSLR-- 2678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 83 eIIDLRTNIDPHGTAQALMQADLQQDLRVDSGkPLVFHQLIQVADNRWYWYQRYHHLLVDGFSFPAITRQIANIYCTWLR 162
Cdd:PRK12316 2679 -IVLEDCAGVADAAIRQRVAEEIQRPFDLARG-PLLRVRLLALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGARR 2756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 163 GEPTPASPFT-PFADVVEEYQQYRESEAWQRDAAFWAEQRRQLPPPASLSPAPLPGRSASADILRLKLEFTDGEFRQL-- 239
Cdd:PRK12316 2757 GEQPTLPPLPlQYADYAAWQRAWMDSGEGARQLDYWRERLGGEQPVLELPLDRPRPALQSHRGARLDVALDVALSRELla 2836
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 240 ATQLSGVQRTDLALALAALWLGRLCNRMDYAAGFIFMRRLGSAALTATGPVLNVLPLGIHIAAQETLPELATRLAAQLKK 319
Cdd:PRK12316 2837 LARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRAETERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQALG 2916
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 320 MRRHQRYDAEQIVR--DSGRAAGDEPLFGPVLNIKVF---DYQLDIPDVQAQTHTLATGPVnDLELALFPDVHGdLSIEI 394
Cdd:PRK12316 2917 AQAHQDLPFEQLVEalQPERSLSHSPLFQVMYNHQSGeraAAQLPGLHIESFAWDGAATQF-DLALDTWESAEG-LGASL 2994
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 395 LANKQRYDEPTLIQHAERLKMLIAQFAADPALLCGDVDIMLPGEYAQLAQ-LNATQVEIP-ETTLSALVAEQAAKTPDAP 472
Cdd:PRK12316 2995 TYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEERGQLLEaWNATAAEYPlERGVHRLFEEQVERTPDAV 3074
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 473 ALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDAR 552
Cdd:PRK12316 3075 ALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSG 3154
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 553 PSLLITTDD-QLPRFSDVPNLtsLCYNAPLTPQGSAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHY 631
Cdd:PRK12316 3155 AQLLLSQSHlRLPLAQGVQVL--DLDRGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAY 3232
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 632 PLTGEDVVAQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPQtarq 711
Cdd:PRK12316 3233 GLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAH---- 3308
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 712 SCATLKQVFCSGEALPADLCREWqqLTGAPLHNLYGPTEAAVDVSWYPAFGEELAQVrgssvPIGYPVWNTGLRILDAMM 791
Cdd:PRK12316 3309 RCTSLKRIVCGGEALPADLQQQV--FAGLPLYNLYGPTEATITVTHWQCVEEGKDAV-----PIGRPIANRACYILDGSL 3381
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 792 HPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGE 871
Cdd:PRK12316 3382 EPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGE 3461
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 872 IDRVMQALPDVEQAVTHACvinqaaatggDARQLVGYLVSQSGLPLDTSALQAQLRETLPPHMVPVVLLQLPQLPLSANG 951
Cdd:PRK12316 3462 IEARLLEHPWVREAVVLAV----------DGRQLVAYVVPEDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNG 3531
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 952 KLDRKALPLPELKAQAPGR-APKAGSETIIAAAFSSLLGCDVQDADADFFALGGHSLLAMKLAAQlSRQVARQVTPGQVM 1030
Cdd:PRK12316 3532 KLDRKALPRPDAALLQQDYvAPVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIISLQVVSR-ARQAGIRFTPKDLF 3610
|
1050
....*....|.
gi 16128569 1031 VASTVAKLATI 1041
Cdd:PRK12316 3611 QHQTIQGLARV 3621
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
482-886 |
1.00e-147 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 452.49 E-value: 1.00e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 482 SYREMREQVVALANLLRER-GVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTD 560
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 561 DQLPRFSDVPNLTSLCYNAPLTPQGSAPLQ-----LSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTG 635
Cdd:TIGR01733 81 ALASRLAGLVLPVILLDPLELAALDDAPAPpppdaPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 636 EDVVAQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFF-AEYGVTTTHFVPSMLAAFVASltpqtARQSCA 714
Cdd:TIGR01733 161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALiAEHPVTVLNLTPSLLALLAAA-----LPPALA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 715 TLKQVFCSGEALPADLCREWQQLTG-APLHNLYGPTEAAVDVSWYPAFGEELAqvRGSSVPIGYPVWNTGLRILDAMMHP 793
Cdd:TIGR01733 236 SLRLVILGGEALTPALVDRWRARGPgARLINLYGPTETTVWSTATLVDPDDAP--RESPVPIGRPLANTRLYVLDDDLRP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 794 VPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAP--GERMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGE 871
Cdd:TIGR01733 314 VPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPFAGgdGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGE 393
|
410
....*....|....*
gi 16128569 872 IDRVMQALPDVEQAV 886
Cdd:TIGR01733 394 IEAALLRHPGVREAV 408
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
461-959 |
5.10e-141 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 437.93 E-value: 5.10e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 461 VAEQAAKTPDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYP 540
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 541 DDRLKMMLEDARPSLLITTDDQLPRFSDVPNLTSLCYNAPLTPQGSAPLQLS-QPHHTAYIIFTSGSTGRPKGVMVGQTA 619
Cdd:cd17651 81 AERLAFMLADAGPVLVLTHPALAGELAVELVAVTLLDQPGAAAGADAEPDPAlDADDLAYVIYTSGSTGRPKGVVMPHRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 620 IVNRLLWMQNHYPLTGEDVVAQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLAA 699
Cdd:cd17651 161 LANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALRA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 700 FVASLTPQTARQscATLKQVFCSGEALPAD-LCREW-QQLTGAPLHNLYGPTEAAVdvswypAFGEELAQV---RGSSVP 774
Cdd:cd17651 241 LAEHGRPLGVRL--AALRYLLTGGEQLVLTeDLREFcAGLPGLRLHNHYGPTETHV------VTALSLPGDpaaWPAPPP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 775 IGYPVWNTGLRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDNGAVEYLG 854
Cdd:cd17651 313 IGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 855 RSDDQLKIRGQRIELGEIDRVMQALPDVEQAVthacVINQAAATGGdaRQLVGYLVSQSGLPLDTSALQAQLRETLPPHM 934
Cdd:cd17651 393 RADDQVKIRGFRIELGEIEAALARHPGVREAV----VLAREDRPGE--KRLVAYVVGDPEAPVDAAELRAALATHLPEYM 466
|
490 500
....*....|....*....|....*
gi 16128569 935 VPVVLLQLPQLPLSANGKLDRKALP 959
Cdd:cd17651 467 VPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
46-1048 |
1.12e-140 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 475.99 E-value: 1.12e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 46 RAVVAGLAQADTLRMRFTEDNG--EVWQWVDDALtfELP-EIIDLRTNIDPHGTAQALMQADLQQDLRVDSgKPLVFHQL 122
Cdd:PRK12316 1597 AAWQATVDRHEILRSGFLWQDGleQPLQVIHKQV--ELPfAELDWRGREDLGQALDALAQAERQKGFDLTR-APLLRLVL 1673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 123 IQVADNRWYWYQRYHHLLVDGFSFPAITRQIANIYCtwlrGEPtPASPFTpfadvveeyqQYRESEAW--QRDA----AF 196
Cdd:PRK12316 1674 VRTGEGRHHLIYTNHHILMDGWSNAQLLGEVLQRYA----GQP-VAAPGG----------RYRDYIAWlqRQDAaaseAF 1738
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 197 WAEQ--RRQLPPPASLSPAPLPGRSASADILRLkleFTDGEFRQLATqLSGVQRTDLALALAALW---LGRLCNRMDYAA 271
Cdd:PRK12316 1739 WKEQlaALEEPTRLAQAARTEDGQVGYGDHQQL---LDPAQTRALAE-FARAQKVTLNTLVQAAWlllLQRYTGQETVAF 1814
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 272 GFIFMRRlgSAALTAT----GPVLNVLPLGIHIAAQETLPELATRLAAQLKKMRRHQRYDAEQIVRDSGRaaGDEPLFGP 347
Cdd:PRK12316 1815 GATVAGR--PAELPGIeqqiGLFINTLPVIAAPRPDQSVADWLQEVQALNLALREHEHTPLYDIQRWAGQ--GGEALFDS 1890
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 348 VLnikVFD-YQLDIPDVQAQTHTLATGPVNDLELALFP-----DVHGDLSIEILANKQRYDEPTLIQHAERLKMLIAQFA 421
Cdd:PRK12316 1891 LL---VFEnYPVAEALKQGAPAGLVFGRVSNHEQTNYPltlavTLGETLSLQYSYDRGHFDAAAIERLDRHLLHLLEQMA 1967
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 422 ADPALLCGDVDIMLPGEYA-QLAQLNATQVEIP-ETTLSALVAEQAAKTPDAPALADARYLFSYREMREQVVALANLLRE 499
Cdd:PRK12316 1968 EDAQAALGELALLDAGERQrILADWDRTPEAYPrGPGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRA 2047
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 500 RGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTDDQLPRFSDVPNLTSLCYNA 579
Cdd:PRK12316 2048 RGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERLPLPAGVARLPLDR 2127
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 580 PLTPQGS---APLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTGEDVVAQKTPCSFDVSVWEFFW 656
Cdd:PRK12316 2128 DAEWADYpdtAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFH 2207
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 657 PFIAGAKLVMaEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPQTARQScatLKQVFCSGEALPADLCRE-WQ 735
Cdd:PRK12316 2208 PLLNGARVLI-RDDELWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDGRPPA---VRVYCFGGEAVPAASLRLaWE 2283
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 736 QLTGAPLHNLYGPTEAAVDVSWYPAFGEELAQVRGssVPIGYPVWNTGLRILDAMMHPVPPGVAGDLYLTGIQLAQGYLG 815
Cdd:PRK12316 2284 ALRPVYLFNGYGPTEAVVTPLLWKCRPQDPCGAAY--VPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLN 2361
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 816 RPDLTASRFIADPF-APGERMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQAVthacVINQ 894
Cdd:PRK12316 2362 RPGLTAERFVPDPFsASGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAV----VVAQ 2437
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 895 AAATGgdaRQLVGYLVSQSGLPLDTSALQAQLRETLPPHMVPVVLLQLPQLPLSANGKLDRKALPLPEL-KAQAPGRAPK 973
Cdd:PRK12316 2438 DGASG---KQLVAYVVPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVsQLRQAYVAPQ 2514
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128569 974 AGSETIIAAAFSSLLGCDVQDADADFFALGGHSLLAMKLAAQLSRQVARQVTPGQVMVASTVAKLATIIDAEEDS 1048
Cdd:PRK12316 2515 EGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVRQDLGLEVPLRILFERPTLAAFAASLESGQTS 2589
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
459-958 |
8.94e-139 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 432.01 E-value: 8.94e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 459 ALVAEQAAKTPDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTG 538
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 539 YPDDRLKMMLEDARPSLLITtDDQLPRFSDVPNLTSLCYNAPLTPQGSAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQT 618
Cdd:cd12117 81 LPAERLAFMLADAGAKVLLT-DRSLAGRAGGLEVAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 619 AIVnRLLWMQNHYPLTGEDVVAQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTThFVPSMLA 698
Cdd:cd12117 160 GVV-RLVKNTNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVL-WLTAALF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 699 AFVASLTPQtarqSCATLKQVFCSGEALPADLCREW-QQLTGAPLHNLYGPTEAAVDVSWYPAfgEELAQVRGSsVPIGY 777
Cdd:cd12117 238 NQLADEDPE----CFAGLRELLTGGEVVSPPHVRRVlAACPGLRLVNGYGPTENTTFTTSHVV--TELDEVAGS-IPIGR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 778 PVWNTGLRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDNGAVEYLGRSD 857
Cdd:cd12117 311 PIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRID 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 858 DQLKIRGQRIELGEIDRVMQALPDVEQAVthacVINQAAATGGdaRQLVGYLVsqSGLPLDTSALQAQLRETLPPHMVPV 937
Cdd:cd12117 391 DQVKIRGFRIELGEIEAALRAHPGVREAV----VVVREDAGGD--KRLVAYVV--AEGALDAAELRAFLRERLPAYMVPA 462
|
490 500
....*....|....*....|.
gi 16128569 938 VLLQLPQLPLSANGKLDRKAL 958
Cdd:cd12117 463 AFVVLDELPLTANGKVDRRAL 483
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
469-958 |
1.39e-138 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 430.94 E-value: 1.39e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 469 PDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMML 548
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 549 EDARPSLLITTDDQLPRFSDVPNLTSLCYNAPlTPQGSAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQ 628
Cdd:cd12116 81 EDAEPALVLTDDALPDRLPAGLPVLLLALAAA-AAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 629 NHYPLTGEDVVAQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPS---MLAAfvaslT 705
Cdd:cd12116 160 ERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPAtwrMLLD-----A 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 706 PQTARQSCATLkqvfCSGEALPADLCREWQQLTGApLHNLYGPTEAAVdvsWYPAfgeelAQVRGSS--VPIGYPVWNTG 783
Cdd:cd12116 235 GWQGRAGLTAL----CGGEALPPDLAARLLSRVGS-LWNLYGPTETTI---WSTA-----ARVTAAAgpIPIGRPLANTQ 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 784 LRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFA-PGERMYRTGDVARWLDNGAVEYLGRSDDQLKI 862
Cdd:cd12116 302 VYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAgPGSRLYRTGDLVRRRADGRLEYLGRADGQVKI 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 863 RGQRIELGEIDRVMQALPDVEQAVThacvinqAAATGGDARQLVGYLVSQSGLPLDTSALQAQLRETLPPHMVPVVLLQL 942
Cdd:cd12116 382 RGHRIELGEIEAALAAHPGVAQAAV-------VVREDGGDRRLVAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVRL 454
|
490
....*....|....*.
gi 16128569 943 PQLPLSANGKLDRKAL 958
Cdd:cd12116 455 DALPLTANGKLDRKAL 470
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
6-1044 |
4.06e-138 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 468.28 E-value: 4.06e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 6 PLVAAQPGIWMAEKLSELPSAWSVAHYVELTGeVDSPLLARAVVAGLAQADTLRMRFTE--DNGEVWQWVDDALTFELPE 83
Cdd:PRK12316 4104 PLSPMQQGMLFHSLYEQEAGDYINQMRVDVQG-LDVERFRAAWQAALDRHDVLRSGFVWqgELGRPLQVVHKQVSLPFAE 4182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 84 IiDLRTNIDPHGTAQALMQADLQQDLRVdSGKPLVFHQLIQVADNRWYWYQRYHHLLVDGFSFPAITRQIANIYctwlRG 163
Cdd:PRK12316 4183 L-DWRGRADLQAALDALAAAERERGFDL-QRAPLLRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLGEVLERY----SG 4256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 164 EPtPASPFTPFADVVEEYQQYRESEAwqrdAAFWAEQRRQLPPPASLSPAPLPGRSASADILRLKLEFTDGEFRQLATQL 243
Cdd:PRK12316 4257 RP-PAQPGGRYRDYIAWLQRQDAAAS----EAFWREQLAALDEPTRLAQAIARADLRSANGYGEHVRELDATATARLREF 4331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 244 SGVQRTDLALALAALW---LGRLCNRMDYAAGFIFMRRlgSAALTAT----GPVLNVLPLGIHIAAQETLPELATRLAAQ 316
Cdd:PRK12316 4332 ARTQRVTLNTLVQAAWlllLQRYTGQDTVAFGATVAGR--PAELPGIegqiGLFINTLPVIATPRAQQSVVEWLQQVQRQ 4409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 317 LKKMRRHQRYDAEQIVRDSGRaaGDEPLFGPVLNIKVfdYQLDIPDVQAQTHTLATGPVNDLE-----LALFPDVHGDLS 391
Cdd:PRK12316 4410 NLALREHEHTPLYEIQRWAGQ--GGEALFDSLLVFEN--YPVSEALQQGAPGGLRFGEVTNHEqtnypLTLAVGLGETLS 4485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 392 IEILANKQRYDEPTLIQHAERLKMLIAQFAADPALLCGDVDIMLPGEY-AQLAQLNATQVEIPET-TLSALVAEQAAKTP 469
Cdd:PRK12316 4486 LQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQqRIVALWNRTDAGYPATrCVHQLVAERARMTP 4565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 470 DAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLE 549
Cdd:PRK12316 4566 DAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMME 4645
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 550 DARPSLLITTDDQLPRFSDVPNLTSLCYNAPLTPQG---SAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLW 626
Cdd:PRK12316 4646 DSGAALLLTQSHLLQRLPIPDGLASLALDRDEDWEGfpaHDPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHA 4725
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 627 MQNHYPLTGEDVVAQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHrDPLAMQQFFAEYGVTTTHFVPSMLAAFvasLTP 706
Cdd:PRK12316 4726 TGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLW-DPERLYAEIHEHRVTVLVFPPVYLQQL---AEH 4801
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 707 QTARQSCATLKQVFCSGEALPADLCRE-WQQLTGAPLHNLYGPTEAAVDVSWYPAFGEELAQVrgSSVPIGYPVWNTGLR 785
Cdd:PRK12316 4802 AERDGEPPSLRVYCFGGEAVAQASYDLaWRALKPVYLFNGYGPTETTVTVLLWKARDGDACGA--AYMPIGTPLGNRSGY 4879
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 786 ILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPF-APGERMYRTGDVARWLDNGAVEYLGRSDDQLKIRG 864
Cdd:PRK12316 4880 VLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgAPGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRG 4959
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 865 QRIELGEIDRVMQALPDVEQAVthacVINQAAATGgdaRQLVGYLVSQSGLPLDTSALQAQLR--------ETLPPHMVP 936
Cdd:PRK12316 4960 FRIELGEIEARLREHPAVREAV----VIAQEGAVG---KQLVGYVVPQDPALADADEAQAELRdelkaalrERLPEYMVP 5032
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 937 VVLLQLPQLPLSANGKLDRKALPLPELK-AQAPGRAPKAGSETIIAAAFSSLLGCDVQDADADFFALGGHSLLAMKLAAQ 1015
Cdd:PRK12316 5033 AHLVFLARMPLTPNGKLDRKALPQPDASlLQQAYVAPRSELEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQVTSR 5112
|
1050 1060
....*....|....*....|....*....
gi 16128569 1016 LSRQVARQVTPGQVMVASTVAKLATIIDA 1044
Cdd:PRK12316 5113 IQLELGLELPLRELFQTPTLAAFVELAAA 5141
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
469-958 |
6.32e-136 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 422.87 E-value: 6.32e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 469 PDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMML 548
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 549 EDARPSLLITtddqlprfsdvpnltslcynapltpqgsaplqlsQPHHTAYIIFTSGSTGRPKGVMVGQtAIVNRLLWMQ 628
Cdd:cd17643 81 ADSGPSLLLT----------------------------------DPDDLAYVIYTSGSTGRPKGVVVSH-ANVLALFAAT 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 629 NH-YPLTGEDVVAQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPQ 707
Cdd:cd17643 126 QRwFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRD 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 708 TARQScaTLKQVFCSGEALPADLCREWQQLTGAP---LHNLYGPTEAAVDVSWYPAFGEELAQVRGSsvPIGYPVWNTGL 784
Cdd:cd17643 206 GRDPL--ALRYVIFGGEALEAAMLRPWAGRFGLDrpqLVNMYGITETTVHVTFRPLDAADLPAAAAS--PIGRPLPGLRV 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 785 RILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPF-APGERMYRTGDVARWLDNGAVEYLGRSDDQLKIR 863
Cdd:cd17643 282 YVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFgGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIR 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 864 GQRIELGEIDRVMQALPDVEQAVthacVINQAAATGGDarQLVGYLVSQSGLPLDTSALQAQLRETLPPHMVPVVLLQLP 943
Cdd:cd17643 362 GFRIELGEIEAALATHPSVRDAA----VIVREDEPGDT--RLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLD 435
|
490
....*....|....*
gi 16128569 944 QLPLSANGKLDRKAL 958
Cdd:cd17643 436 ALPLTVNGKLDRAAL 450
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
460-962 |
1.61e-132 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 415.57 E-value: 1.61e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 460 LVAEQAAKTPDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGY 539
Cdd:cd17655 2 LFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 540 PDDRLKMMLEDARPSLLITTDDQLPRFSDVPNLTSLCYNApLTPQGSAPLQ-LSQPHHTAYIIFTSGSTGRPKGVMVGQT 618
Cdd:cd17655 82 PEERIQYILEDSGADILLTQSHLQPPIAFIGLIDLLDEDT-IYHEESENLEpVSKSDDLAYVIYTSGSTGKPKGVMIEHR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 619 AIVNRLLWMQNHYPLTGEDVVAQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLa 698
Cdd:cd17655 161 GVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAHL- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 699 afvaSLTPQTARQSCATLKQVFCSGEALPADLCREWQQL--TGAPLHNLYGPTEAAVDVSWYPAfgeELAQVRGSSVPIG 776
Cdd:cd17655 240 ----KLLDAADDSEGLSLKHLIVGGEALSTELAKKIIELfgTNPTITNAYGPTETTVDASIYQY---EPETDQQVSVPIG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 777 YPVWNTGLRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDNGAVEYLGRS 856
Cdd:cd17655 313 KPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 857 DDQLKIRGQRIELGEIDRVMQALPDVEQAVthacVINQAAATGGDarQLVGYLVSQSglPLDTSALQAQLRETLPPHMVP 936
Cdd:cd17655 393 DHQVKIRGYRIELGEIEARLLQHPDIKEAV----VIARKDEQGQN--YLCAYIVSEK--ELPVAQLREFLARELPDYMIP 464
|
490 500
....*....|....*....|....*.
gi 16128569 937 VVLLQLPQLPLSANGKLDRKALPLPE 962
Cdd:cd17655 465 SYFIKLDEIPLTPNGKVDRKALPEPD 490
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
469-959 |
1.53e-128 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 402.79 E-value: 1.53e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 469 PDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMML 548
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 549 EDARPSLLITtddqlprfsdvpnltslcynapltpqgsaplqlsQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQ 628
Cdd:cd17652 81 ADARPALLLT----------------------------------TPDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 629 NHYPLTGEDVVAQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPQt 708
Cdd:cd17652 127 AAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAALPPDDLPD- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 709 arqscatLKQVFCSGEALPADLCREWQQltGAPLHNLYGPTEAAVDVSWYPAFGEelaqvrGSSVPIGYPVWNTGLRILD 788
Cdd:cd17652 206 -------LRTLVVAGEACPAELVDRWAP--GRRMINAYGPTETTVCATMAGPLPG------GGVPPIGRPVPGTRVYVLD 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 789 AMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPF-APGERMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRI 867
Cdd:cd17652 271 ARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFgAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRI 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 868 ELGEIDRVMQALPDVEQAVthacVINQAAATGGdaRQLVGYLVSQSGLPLDTSALQAQLRETLPPHMVPVVLLQLPQLPL 947
Cdd:cd17652 351 ELGEVEAALTEHPGVAEAV----VVVRDDRPGD--KRLVAYVVPAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPL 424
|
490
....*....|..
gi 16128569 948 SANGKLDRKALP 959
Cdd:cd17652 425 TPNGKLDRRALP 436
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
1-442 |
6.27e-124 |
|
Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.
Pssm-ID: 395541 [Multi-domain] Cd Length: 454 Bit Score: 391.31 E-value: 6.27e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 1 MSQHLPLVAAQPGIWMAEKLSELPSAWSVAHYVELTGEVDSPLLARAVVAGLAQADTLRMRFTED-NGEVWQWVDDALTF 79
Cdd:pfam00668 1 VQDEYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQeNGEPVQVILEERPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 80 ELpEIIDLR--TNIDPHGTAQALMQADLQQDLRVDSGkPLVFHQLIQVADNRWYWYQRYHHLLVDGFSFPAITRQIANIY 157
Cdd:pfam00668 81 EL-EIIDISdlSESEEEEAIEAFIQRDLQSPFDLEKG-PLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 158 CTWLRGEPTPASPFTPFADVVEEYQQYRESEAWQRDAAFWAEQRRQLPPPAS--LSPAPLPGRSASADILRLKLEFTDGE 235
Cdd:pfam00668 159 QQLLKGEPLPLPPKTPYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQlpKDYARPADRSFKGDRLSFTLDEDTEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 236 FRQLATQLSGVQRTDLALALAALWLGRLCNRMDYAAGFIFMRRLGSAALTATGPVLNVLPLGIHIAAQETLPELATRLAA 315
Cdd:pfam00668 239 LLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 316 QLKKMRRHQRYDAEQIVRDSG--RAAGDEPLFGPVLNIKVFDYQldipDVQAQTHTLATGPVN-----------DLELAL 382
Cdd:pfam00668 319 DLLSAEPHQGYPFGDLVNDLRlpRDLSRHPLFDPMFSFQNYLGQ----DSQEEEFQLSELDLSvssvieeeakyDLSLTA 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 383 FPDvHGDLSIEILANKQRYDEPTLIQHAERLKMLIAQFAADPALLCGDVDIMLPGEYAQL 442
Cdd:pfam00668 395 SER-GGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKL 453
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
460-958 |
4.06e-121 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 383.59 E-value: 4.06e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 460 LVAEQAAKTPDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGY 539
Cdd:cd12115 4 LVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 540 PDDRLKMMLEDARPSLLITtddqlprfsdvpnltslcynapltpqgsaplqlsQPHHTAYIIFTSGSTGRPKGVMVGQTA 619
Cdd:cd12115 84 PPERLRFILEDAQARLVLT----------------------------------DPDDLAYVIYTSGSTGRPKGVAIEHRN 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 620 IVNRLLWMQNHYP---LTGedvVAQKTPCSFDVSVWEFFWPFIAGAKLVMAEpeahrDPLAMQQFFAEYGVTTTHFVPSM 696
Cdd:cd12115 130 AAAFLQWAAAAFSaeeLAG---VLASTSICFDLSVFELFGPLATGGKVVLAD-----NVLALPDLPAAAEVTLINTVPSA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 697 LAAFV-ASLTPQTARQscatlkqVFCSGEALPADLCRE-WQQLTGAPLHNLYGPTEAAVdvswYpAFGEELAQVRGSSVP 774
Cdd:cd12115 202 AAELLrHDALPASVRV-------VNLAGEPLPRDLVQRlYARLQVERVVNLYGPSEDTT----Y-STVAPVPPGASGEVS 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 775 IGYPVWNTGLRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDNGAVEYLG 854
Cdd:cd12115 270 IGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLG 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 855 RSDDQLKIRGQRIELGEIDRVMQALPDVEQAVthacvinqAAATGGDA--RQLVGYLVSQSGLPLDTSALQAQLRETLPP 932
Cdd:cd12115 350 RADNQVKVRGFRIELGEIEAALRSIPGVREAV--------VVAIGDAAgeRRLVAYIVAEPGAAGLVEDLRRHLGTRLPA 421
|
490 500
....*....|....*....|....*.
gi 16128569 933 HMVPVVLLQLPQLPLSANGKLDRKAL 958
Cdd:cd12115 422 YMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
469-959 |
4.28e-117 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 372.86 E-value: 4.28e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 469 PDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMML 548
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 549 EDARPSLLITTDdqlprfsdvpnltslcynapltpqgsaplqlsqPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQ 628
Cdd:cd17649 81 EDSGAGLLLTHH---------------------------------PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 629 NHYPLTGEDVVAQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPQT 708
Cdd:cd17649 128 ERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEADRTG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 709 ARqSCATLKQVFCSGEALPADLCREWQQlTGAPLHNLYGPTEAAVDVSWYPAfgEELAQVRGSSVPIGYPVWNTGLRILD 788
Cdd:cd17649 208 DG-RPPSLRLYIFGGEALSPELLRRWLK-APVRLFNAYGPTEATVTPLVWKC--EAGAARAGASMPIGRPLGGRSAYILD 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 789 AMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPF-APGERMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRI 867
Cdd:cd17649 284 ADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFgAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRI 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 868 ELGEIDRVMQALPdveqAVTHACVINQAAATGGdarQLVGYLVSQSG--LPLDTSALQAQLRETLPPHMVPVVLLQLPQL 945
Cdd:cd17649 364 ELGEIEAALLEHP----GVREAAVVALDGAGGK---QLVAYVVLRAAaaQPELRAQLRTALRASLPDYMVPAHLVFLARL 436
|
490
....*....|....
gi 16128569 946 PLSANGKLDRKALP 959
Cdd:cd17649 437 PLTPNGKLDRKALP 450
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
456-959 |
1.35e-115 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 369.46 E-value: 1.35e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 456 TLSALVAEQAAKTPDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPL 535
Cdd:cd17644 1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 536 DTGYPDDRLKMMLEDARPSLLITtddqlprfsdvpnltslcynapltpqgsaplqlsQPHHTAYIIFTSGSTGRPKGVMV 615
Cdd:cd17644 81 DPNYPQERLTYILEDAQISVLLT----------------------------------QPENLAYVIYTSGSTGKPKGVMI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 616 GQTAIVNRLLWMQNHYPLTGEDVVAQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPS 695
Cdd:cd17644 127 EHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 696 MLAAFVASLTPQTArQSCATLKQVFCSGEALPADLCREWQQLTG--APLHNLYGPTEAAVDVSWYPAFGEELAQVrgSSV 773
Cdd:cd17644 207 YWHLLVLELLLSTI-DLPSSLRLVIVGGEAVQPELVRQWQKNVGnfIQLINVYGPTEATIAATVCRLTQLTERNI--TSV 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 774 PIGYPVWNTGLRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFA--PGERMYRTGDVARWLDNGAVE 851
Cdd:cd17644 284 PIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNssESERLYKTGDLARYLPDGNIE 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 852 YLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQavthACVINQAAATGGdaRQLVGYLVSQSGLPLDTSALQAQLRETLP 931
Cdd:cd17644 364 YLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKT----AVVIVREDQPGN--KRLVAYIVPHYEESPSTVELRQFLKAKLP 437
|
490 500
....*....|....*....|....*...
gi 16128569 932 PHMVPVVLLQLPQLPLSANGKLDRKALP 959
Cdd:cd17644 438 DYMIPSAFVVLEELPLTPNGKIDRRALP 465
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
469-958 |
8.85e-114 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 365.06 E-value: 8.85e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 469 PDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMML 548
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 549 EDARPSLLITtDDQLPRFSDVPNLTSLCYNAPLTPQGSAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQ 628
Cdd:cd12114 81 ADAGARLVLT-DGPDAQLDVAVFDVLILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDIN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 629 NHYPLTGEDVVAQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPS---MLAAFVASlt 705
Cdd:cd12114 160 RRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPAlleMLLDVLEA-- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 706 PQTARQScatLKQVFCSGEALPADLCREWQQLT-GAPLHNLYGPTEAAVDVSWYPaFGEELAQVRgsSVPIGYPVWNTGL 784
Cdd:cd12114 238 AQALLPS---LRLVLLSGDWIPLDLPARLRALApDARLISLGGATEASIWSIYHP-IDEVPPDWR--SIPYGRPLANQRY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 785 RILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPfaPGERMYRTGDVARWLDNGAVEYLGRSDDQLKIRG 864
Cdd:cd12114 312 RVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 865 QRIELGEIDRVMQALPDVEQAVThacvinqAAATGGDARQLVGYLVSQSGLPLDTS-ALQAQLRETLPPHMVPVVLLQLP 943
Cdd:cd12114 390 YRIELGEIEAALQAHPGVARAVV-------VVLGDPGGKRLAAFVVPDNDGTPIAPdALRAFLAQTLPAYMIPSRVIALE 462
|
490
....*....|....*
gi 16128569 944 QLPLSANGKLDRKAL 958
Cdd:cd12114 463 ALPLTANGKVDRAAL 477
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
461-863 |
2.51e-113 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 361.24 E-value: 2.51e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 461 VAEQAAKTPDAPALADARY-LFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGY 539
Cdd:pfam00501 1 LERQAARTPDKTALEVGEGrRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 540 PDDRLKMMLEDARPSLLITTDDQLP-------------------RFSDVPNLTSLCYNAPLTPQGSAPLQLSQPHHTAYI 600
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALKLeellealgklevvklvlvlDRDPVLKEEPLPEEAKPADVPPPPPPPPDPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 601 IFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYP----LTGEDVVAQKTPCSFDVSV-WEFFWPFIAGAKLVMAEPEAHRDP 675
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPrgfgLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPALDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 676 LAMQQFFAEYGVTTTHFVPSMLAAFVASLTPQTARQScaTLKQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVdV 755
Cdd:pfam00501 241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLS--SLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTG-V 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 756 SWYPAFGEELAQVRGSsvpIGYPVWNTGLRILD-AMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADpfapgeR 834
Cdd:pfam00501 318 VTTPLPLDEDLRSLGS---VGRPLPGTEVKIVDdETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED------G 388
|
410 420
....*....|....*....|....*....
gi 16128569 835 MYRTGDVARWLDNGAVEYLGRSDDQLKIR 863
Cdd:pfam00501 389 WYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
465-958 |
3.75e-109 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 351.16 E-value: 3.75e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 465 AAKTPDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRL 544
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 545 KMMLEDARPSLLITTDDQLprfsdvpnltslcynapltpqgsaplqlsqphhtAYIIFTSGSTGRPKGVMVGQTAIVNRL 624
Cdd:cd05945 81 REILDAAKPALLIADGDDN----------------------------------AYIIFTSGSTGRPKGVQISHDNLVSFT 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 625 LWMQNHYPLTGEDVVAQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLAafVASL 704
Cdd:cd05945 127 NWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAA--MCLL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 705 TPQTARQSCATLKQVFCSGEALPADLCREWQQLT-GAPLHNLYGPTEAAVDVSWYPAFGEELAQVrgSSVPIGYPVWNTG 783
Cdd:cd05945 205 SPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPTEATVAVTYIEVTPEVLDGY--DRLPIGYAKPGAK 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 784 LRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADpfaPGERMYRTGDVARWLDNGAVEYLGRSDDQLKIR 863
Cdd:cd05945 283 LVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPD---EGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLN 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 864 GQRIELGEIDRVMQALPDVEQAVThacvinQAAATGGDARQLVGYLVSQSGLP-LDTSALQAQLRETLPPHMVPVVLLQL 942
Cdd:cd05945 360 GYRIELEEIEAALRQVPGVKEAVV------VPKYKGEKVTELIAFVVPKPGAEaGLTKAIKAELAERLPPYMIPRRFVYL 433
|
490
....*....|....*.
gi 16128569 943 PQLPLSANGKLDRKAL 958
Cdd:cd05945 434 DELPLNANGKIDRKAL 449
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
2-1053 |
1.62e-108 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 379.51 E-value: 1.62e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 2 SQHLPLVAAQPGIWMAEKLSELPSAWSVAHYVELTGEVDSPLLARAVVAGLAQADTLRMRFTEDNGEVWQWVDDALTFEL 81
Cdd:PRK05691 1726 SQPVPLSYSQQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSVDGVPVQQVAEDSGLRM 1805
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 82 pEIIDLRTnIDPHGTAQALMQ-ADLQ--QDLRVDSGkPLVFHQLIQVADNRWYWYQRYHHLLVDGFSFPAITRQIANIYC 158
Cdd:PRK05691 1806 -DWQDFSA-LPADARQQRLQQlADSEahQPFDLERG-PLLRACLVKAAEREHYFVLTLHHIVTEGWAMDIFARELGALYE 1882
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 159 TWLRGEPTPASPF-TPFADVVEEYQQYRESEAWQRDAAFWAEQ--RRQLPPPASLSPAPLPGRSASADILRLKLEFTDGE 235
Cdd:PRK05691 1883 AFLDDRESPLEPLpVQYLDYSVWQRQWLESGERQRQLDYWKAQlgNEHPLLELPADRPRPPVQSHRGELYRFDLSPELAA 1962
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 236 FRQLATQLSGVQRTDLALALAALWLGRLCNRMDYAAGFIFMRRLGSAALTATGPVLNVLPLGIHIAAQETLPELATRLAA 315
Cdd:PRK05691 1963 RVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRIRPESEGLIGAFLNTQVLRCQLDGQMSVSELLEQVRQ 2042
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 316 QLKKMRRHQRYDAEQIVR--DSGRAAGDEPLFGPVLNIKVFDYQldipdvqaQTHTLATGPV----NDLELALFpdvhgD 389
Cdd:PRK05691 2043 TVIEGQSHQDLPFDHLVEalQPPRSAAYNPLFQVMCNVQRWEFQ--------QSRQLAGMTVeylvNDARATKF-----D 2109
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 390 LSIEILANKQR-----------YDEPTLIQHAERLKMLIAQFAADPALLCGDVDIMLPGEYAQL-AQLNATQVEIP-ETT 456
Cdd:PRK05691 2110 LNLEVTDLDGRlgccltysrdlFDEPRIARMAEHWQNLLEALLGDPQQRLAELPLLAAAEQQQLlDSLAGEAGEARlDQT 2189
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 457 LSALVAEQAAKTPDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLD 536
Cdd:PRK05691 2190 LHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLD 2269
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 537 TGYPDDRLKMMLEDARPSLLITTDDQLPRFSDVP-NLTSLCYN---APLTPQGSAPL-QLSQPHHTAYIIFTSGSTGRPK 611
Cdd:PRK05691 2270 PEYPLERLHYMIEDSGIGLLLSDRALFEALGELPaGVARWCLEddaAALAAYSDAPLpFLSLPQHQAYLIYTSGSTGKPK 2349
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 612 GVMVGQTAIVNRLLWMQNHYPLTGEDVVAQKTPCSFDVSVWEFFWPFIAGAKLVMaEPEAHRDPLAMQQFFAEYGVTTTH 691
Cdd:PRK05691 2350 GVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARVVL-RAQGQWGAEEICQLIREQQVSILG 2428
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 692 FVP---SMLAAFVASLTPQTARQSCATlkqvfcSGEAL-PADLCREWQQLTGAPLHNLYGPTEAAVDVSWYPAfGEELAQ 767
Cdd:PRK05691 2429 FTPsygSQLAQWLAGQGEQLPVRMCIT------GGEALtGEHLQRIRQAFAPQLFFNAYGPTETVVMPLACLA-PEQLEE 2501
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 768 VRGsSVPIGYPVWNTGLRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAP-GERMYRTGDVARWLD 846
Cdd:PRK05691 2502 GAA-SVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAAdGGRLYRTGDLVRLRA 2580
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 847 NGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQAVTHAcvinqAAATGGdaRQLVGYLVSQSGLPLDTS------ 920
Cdd:PRK05691 2581 DGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLA-----LDTPSG--KQLAGYLVSAVAGQDDEAqaalre 2653
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 921 ALQAQLRETLPPHMVPVVLLQLPQLPLSANGKLDRKALPLPELKAQAPG-RAPKAGSETIIAAAFSSLLGCDVQDADADF 999
Cdd:PRK05691 2654 ALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPDPELNRQAyQAPRSELEQQLAQIWREVLNVERVGLGDNF 2733
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|....
gi 16128569 1000 FALGGHSLLAMKLAAQlSRQVARQVTPGQVMVASTVAKLATIIDAEEDSTRRMG 1053
Cdd:PRK05691 2734 FELGGDSILSIQVVSR-ARQLGIHFSPRDLFQHQTVQTLAAVATHSEAAQAEQG 2786
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
463-958 |
1.53e-104 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 338.13 E-value: 1.53e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 463 EQAAKTPDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDD 542
Cdd:cd17653 5 RIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 543 RLKMMLEDARPSLLITTDdqlprfsdvpnltslcynapltpqgsaplqlsQPHHTAYIIFTSGSTGRPKGVMVGQTAIVN 622
Cdd:cd17653 85 RIQAILRTSGATLLLTTD--------------------------------SPDDLAYIIFTSGSTGIPKGVMVPHRGVLN 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 623 RLLWMQNHYPLTGEDVVAQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEahrDPLAMqqffAEYGVTTTHFVPSMLAafva 702
Cdd:cd17653 133 YVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLADPS---DPFAH----VARTVDALMSTPSILS---- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 703 SLTPQtarqSCATLKQVFCSGEALPADLCREWqqLTGAPLHNLYGPTEAAVDVSwypafgeeLAQVR-GSSVPIGYPVWN 781
Cdd:cd17653 202 TLSPQ----DFPNLKTIFLGGEAVPPSLLDRW--SPGRRLYNAYGPTECTISST--------MTELLpGQPVTIGKPIPN 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 782 TGLRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDNGAVEYLGRSDDQLK 861
Cdd:cd17653 268 STCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVK 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 862 IRGQRIELGEIDRVMQAL-PDVEQAVthACVINQaaatggdarQLVGYLVSQSglpLDTSALQAQLRETLPPHMVPVVLL 940
Cdd:cd17653 348 VRGFRINLEEIEEVVLQSqPEVTQAA--AIVVNG---------RLVAFVTPET---VDVDGLRSELAKHLPSYAVPDRII 413
|
490
....*....|....*...
gi 16128569 941 QLPQLPLSANGKLDRKAL 958
Cdd:cd17653 414 ALDSFPLTANGKVDRKAL 431
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
460-958 |
1.67e-100 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 328.73 E-value: 1.67e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 460 LVAEQAAKTPDAPALA--DARylFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDT 537
Cdd:cd05918 4 LIEERARSQPDAPAVCawDGS--LTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 538 GYPDDRLKMMLEDARPSLLITtddqlprfsdvpnltslcynapltpqgsaplqlSQPHHTAYIIFTSGSTGRPKGVMVGQ 617
Cdd:cd05918 82 SHPLQRLQEILQDTGAKVVLT---------------------------------SSPSDAAYVIFTSGSTGKPKGVVIEH 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 618 TAIVNRLLWMQNHYPLTGEDVVAQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAmqQFFAEYGVTTTHFVPSml 697
Cdd:cd05918 129 RALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLNDLA--GFINRLRVTWAFLTPS-- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 698 aafVASLTPqtaRQSCATLKQVFCSGEALPADLCREWQQltGAPLHNLYGPTEAAVDVSwypafgeeLAQVRGSSVP--I 775
Cdd:cd05918 205 ---VARLLD---PEDVPSLRTLVLGGEALTQSDVDTWAD--RVRLINAYGPAECTIAAT--------VSPVVPSTDPrnI 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 776 GYPVwNTGLRILDAMMH--PVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADP-------FAPGERMYRTGDVARWLD 846
Cdd:cd05918 269 GRPL-GATCWVVDPDNHdrLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqegSGRGRRLYRTGDLVRYNP 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 847 NGAVEYLGRSDDQLKIRGQRIELGEI-DRVMQALPDVEQAVTHACVInqaaATGGDARQLVGYLVSQSG----------- 914
Cdd:cd05918 348 DGSLEYVGRKDTQVKIRGQRVELGEIeHHLRQSLPGAKEVVVEVVKP----KDGSSSPQLVAFVVLDGSssgsgdgdslf 423
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 16128569 915 ------LPLDTSALQAQLRETLPPHMVPVVLLQLPQLPLSANGKLDRKAL 958
Cdd:cd05918 424 lepsdeFRALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
469-958 |
1.18e-98 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 322.49 E-value: 1.18e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 469 PDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMML 548
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 549 EDArpsllittddqlprfsdvpnltslcynapltpqgSAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQ 628
Cdd:cd17650 81 EDS----------------------------------GAKLLLTQPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWR 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 629 NHYPLTGEDVVA-QKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPQ 707
Cdd:cd17650 127 REYELDSFPVRLlQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAYVYRN 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 708 TARQSCATLKQVFCSGEAL--PADLCREWQQltGAPLHNLYGPTEAAVDVSWYPAFGEELaqVRGSSVPIGYPVWNTGLR 785
Cdd:cd17650 207 GLDLSAMRLLIVGSDGCKAqdFKTLAARFGQ--GMRIINSYGVTEATIDSTYYEEGRDPL--GDSANVPIGRPLPNTAMY 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 786 ILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQ 865
Cdd:cd17650 283 VLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGF 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 866 RIELGEIDRVMQALPDVEQAVthacVINQAAAtGGDARqLVGYLVSQSglPLDTSALQAQLRETLPPHMVPVVLLQLPQL 945
Cdd:cd17650 363 RIELGEIESQLARHPAIDEAV----VAVREDK-GGEAR-LCAYVVAAA--TLNTAELRAFLAKELPSYMIPSYYVQLDAL 434
|
490
....*....|...
gi 16128569 946 PLSANGKLDRKAL 958
Cdd:cd17650 435 PLTPNGKVDRRAL 447
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
460-959 |
2.34e-98 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 321.43 E-value: 2.34e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 460 LVAEQAAKTPDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGY 539
Cdd:cd17645 3 LFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 540 PDDRLKMMLEDArpsllittddqlprfsdvpnltslcynapltpqgSAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTA 619
Cdd:cd17645 83 PGERIAYMLADS----------------------------------SAKILLTNPDDLAYVIYTSGSTGLPKGVMIEHHN 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 620 IVNRLLWMQNHYPLTGEDVVAQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTThFVPSMLAA 699
Cdd:cd17645 129 LVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITIS-FLPTGAAE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 700 FVASLTPQTarqscatLKQVFCSGEALPADLCREWQqltgapLHNLYGPTEAAVDVSWYPAFGEElaqvrgSSVPIGYPV 779
Cdd:cd17645 208 QFMQLDNQS-------LRVLLTGGDKLKKIERKGYK------LVNNYGPTENTVVATSFEIDKPY------ANIPIGKPI 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 780 WNTGLRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDNGAVEYLGRSDDQ 859
Cdd:cd17645 269 DNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQ 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 860 LKIRGQRIELGEIDRVMQALPDVEQAVthacVInqAAATGGDARQLVGYLVSQSGLPLDtsALQAQLRETLPPHMVPVVL 939
Cdd:cd17645 349 VKIRGYRIEPGEIEPFLMNHPLIELAA----VL--AKEDADGRKYLVAYVTAPEEIPHE--ELREWLKNDLPDYMIPTYF 420
|
490 500
....*....|....*....|
gi 16128569 940 LQLPQLPLSANGKLDRKALP 959
Cdd:cd17645 421 VHLKALPLTANGKVDRKALP 440
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
457-958 |
5.02e-96 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 315.60 E-value: 5.02e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 457 LSALVAEQAAKTPDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLD 536
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 537 TGYPDDRLKMMLEDARPSLLITtddqlprfsdvpnltslcynapltpqgsaplqlsqphhtAYIIFTSGSTGRPKGVMVG 616
Cdd:COG0318 81 PRLTAEELAYILEDSGARALVT---------------------------------------ALILYTSGTTGRPKGVMLT 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 617 QTAIVNRLLWMQNHYPLTGEDVVAQKTPCSFDVS-VWEFFWPFIAGAKLVMAEpeaHRDPLAMQQFFAEYGVTTTHFVPS 695
Cdd:COG0318 122 HRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGlTVGLLAPLLAGATLVLLP---RFDPERVLELIERERVTVLFGVPT 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 696 MLAAFVAslTPQTARQSCATLKQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVDVSWYPAfgEELAQVRGSsvpI 775
Cdd:COG0318 199 MLARLLR--HPEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPE--DPGERRPGS---V 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 776 GYPVWNTGLRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFiADPFapgermYRTGDVARWLDNGAVEYLGR 855
Cdd:COG0318 272 GRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGW------LRTGDLGRLDEDGYLYIVGR 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 856 SDDQLKIRGQRIELGEIDRVMQALPDVEQavthACVINQAAATGGDArqLVGYLVSQSGLPLDTSALQAQLRETLPPHMV 935
Cdd:COG0318 345 KKDMIISGGENVYPAEVEEVLAAHPGVAE----AAVVGVPDEKWGER--VVAFVVLRPGAELDAEELRAFLRERLARYKV 418
|
490 500
....*....|....*....|...
gi 16128569 936 PVVLLQLPQLPLSANGKLDRKAL 958
Cdd:COG0318 419 PRRVEFVDELPRTASGKIDRRAL 441
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
468-959 |
6.35e-93 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 307.86 E-value: 6.35e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 468 TPDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMM 547
Cdd:cd17656 1 TPDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 548 LEDARPSLLITTDDQLPRFSDvpNLTSLCYNAPLTPQGSAP-LQLS-QPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLL 625
Cdd:cd17656 81 MLDSGVRVVLTQRHLKSKLSF--NKSTILLEDPSISQEDTSnIDYInNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 626 WMQNHYPLTGEDVVAQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTThFVPSMLAAFVASLT 705
Cdd:cd17656 159 FEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVV-FLPVAFLKFIFSER 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 706 pQTARQSCATLKQVFCSGEALP-ADLCREWQQLTGAPLHNLYGPTEAAVDVSWYPAFGEELAQVRgssvPIGYPVWNTGL 784
Cdd:cd17656 238 -EFINRFPTCVKHIITAGEQLViTNEFKEMLHEHNVHLHNHYGPSETHVVTTYTINPEAEIPELP----PIGKPISNTWI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 785 RILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDNGAVEYLGRSDDQLKIRG 864
Cdd:cd17656 313 YILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 865 QRIELGEIDRVMQALPDVEQAVthacVINQAAATGGdaRQLVGYLVSQSGLPldTSALQAQLRETLPPHMVPVVLLQLPQ 944
Cdd:cd17656 393 YRIELGEIEAQLLNHPGVSEAV----VLDKADDKGE--KYLCAYFVMEQELN--ISQLREYLAKQLPEYMIPSFFVPLDQ 464
|
490
....*....|....*
gi 16128569 945 LPLSANGKLDRKALP 959
Cdd:cd17656 465 LPLTPNGKVDRKALP 479
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
469-959 |
2.56e-92 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 305.48 E-value: 2.56e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 469 PDAPALADARYLFSYREMREQVVALANLLRERG-VKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMM 547
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 548 LEDARPSLLITTDDQLprfsdvpnltslcynapltpqgsaplqlsqphhtAYIIFTSGSTGRPKGVMVGQTAIVNRLLWM 627
Cdd:cd17648 81 LEDTGARVVITNSTDL----------------------------------AYAIYTSGTTGKPKGVLVEHGSVVNLRTSL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 628 QNHYPLTGED--VVAQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASlt 705
Cdd:cd17648 127 SERYFGRDNGdeAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQYDLA-- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 706 pqtarqSCATLKQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVD--VSWYPAfgeeLAQVRGSsvpIGYPVWNTG 783
Cdd:cd17648 205 ------RLPHLKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETTVTnhKRFFPG----DQRFDKS---LGRPVRNTK 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 784 LRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFA-PGE-------RMYRTGDVARWLDNGAVEYLGR 855
Cdd:cd17648 272 CYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQtEQErargrnaRLYKTGDLVRWLPSGELEYLGR 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 856 SDDQLKIRGQRIELGEIDRVMQALPDVEQAVthacVINQAAATGGDARQ---LVGYLVSQSGlPLDTSALQAQLRETLPP 932
Cdd:cd17648 352 NDFQVKIRGQRIEPGEVEAALASYPGVRECA----VVAKEDASQAQSRIqkyLVGYYLPEPG-HVPESDLLSFLRAKLPR 426
|
490 500
....*....|....*....|....*..
gi 16128569 933 HMVPVVLLQLPQLPLSANGKLDRKALP 959
Cdd:cd17648 427 YMVPARLVRLEGIPVTINGKLDVRALP 453
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
395-1048 |
1.29e-87 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 315.18 E-value: 1.29e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 395 LANKQRY-DEPT---LIQHAERLKMLIAQ-FAADPAllcgdvDIMLPGEYAQ---LAQLNATQVEIP-ETTLSALVAEQA 465
Cdd:PRK05691 3657 LSYDQRYfDAPTverLLGEFKRLLLALVQgFHGDLS------ELPLLGEQERdflLDGCNRSERDYPlEQSYVRLFEAQV 3730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 466 AKTPD--APALADARYlfSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDR 543
Cdd:PRK05691 3731 AAHPQriAASCLDQQW--SYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQR 3808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 544 LKMMLEDARPSLLITTDDQLPRFSDVPNLTSlCYNAPL------TPQGSA----PLQLSQPHHTAYIIFTSGSTGRPKGV 613
Cdd:PRK05691 3809 LQRIIELSRTPVLVCSAACREQARALLDELG-CANRPRllvweeVQAGEVashnPGIYSGPDNLAYVIYTSGSTGLPKGV 3887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 614 MVGQTAIVNRLLWMQNHYPLTGEDVVAQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFV 693
Cdd:PRK05691 3888 MVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIAHDPQGLLAHVQAQGITVLESV 3967
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 694 PSMLAAFVASltpqtARQSCATLKQVFCSGEALPADLCREW-QQLTGAPLHNLYGPTEAAVDVSWYPAfgeELAQVRGSS 772
Cdd:PRK05691 3968 PSLIQGMLAE-----DRQALDGLRWMLPTGEAMPPELARQWlQRYPQIGLVNAYGPAECSDDVAFFRV---DLASTRGSY 4039
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 773 VPIGYPVWNTGLRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPF-APGERMYRTGDVARWLDNGAVE 851
Cdd:PRK05691 4040 LPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgAPGERLYRTGDLARRRSDGVLE 4119
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 852 YLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQAVthacVINQAAATGgdaRQLVGYLVSQSGlPLDTSAL----QAQLR 927
Cdd:PRK05691 4120 YVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAA----VAVQEGVNG---KHLVGYLVPHQT-VLAQGALleriKQRLR 4191
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 928 ETLPPHMVPVVLLQLPQLPLSANGKLDRKALPLPELKAQAPG--RAPKAGSETIIAAAFSSLLGCDVQDADADFFALGGH 1005
Cdd:PRK05691 4192 AELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQLQSQayLAPRNELEQTLATIWADVLKVERVGVHDNFFELGGH 4271
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 16128569 1006 SLLAMKLAAQLSRQVARQVTPGQVMVASTVAKLATIIDAEEDS 1048
Cdd:PRK05691 4272 SLLATQIASRVQKALQRNVPLRAMFECSTVEELAEYIEGLAGS 4314
|
|
| EntF2 |
COG3319 |
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ... |
459-1293 |
5.67e-68 |
|
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442548 [Multi-domain] Cd Length: 855 Bit Score: 246.92 E-value: 5.67e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 459 ALVAEQAAKTPDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTG 538
Cdd:COG3319 5 AAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAALAAL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 539 YPDDRLKMMLEDARPSLLITTDDQLPRfSDVPNLTSLCYNAPLTPQGSAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQT 618
Cdd:COG3319 85 ALALAAAAAALLLAALALLLALLAALA-LALLALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGGAGV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 619 AIVNRLLWMQNHYPLTGEDVVAQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLA 698
Cdd:COG3319 164 LVLVLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALLLLL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 699 AFVASLTPQTARQSCATLKQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVDVSWYPAFGEELAQVRGSSVPIGYP 778
Cdd:COG3319 244 LAALLLLLALALLLLLALLLLLGLLALLLALLLLLALLLLAAAAALAAGGTATTAAVTTTAAAAAPGVAGALGPIGGGPG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 779 VWNTGLRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDNGAVEYLGRSDD 858
Cdd:COG3319 324 LLVLLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAGAGARGRLRRGGDRGRRLGGGLLLGLGRLRL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 859 QLKIRGQRIELGEIDRVMQALPDVEQAVthacvinQAAATGGDARQLVGYLVSQSGLPLDTSALQAQLRETLPPHMVPVV 938
Cdd:COG3319 404 QRLRRGLREELEEAEAALAEAAAVAAAV-------AAAAAAAAAAAALAAAVVAAAALAAAALLLLLLLLLLPPPLPPAL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 939 LLQLPQLPLSANGKLDRKALPLPELKAQAPGRAPKAGSETIIAAAFSSLLGCDVQDADADFFALGGHSLLAMKLAAQLSR 1018
Cdd:COG3319 477 LLLLLLLLLLLLAALLLAAAAPAAAAAAAAAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLLA 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 1019 QVARQVTPGQVMVASTVAKLATIIDAEEDSTRrmGFETILPLREGNGPTLFCFHPASGFAWQFSVLSRYLDPQWSIIGIQ 1098
Cdd:COG3319 557 LLLRLLLLLALLLAPTLAALAAALAAAAAAAA--LSPLVPLRAGGSGPPLFCVHPAGGNVLCYRPLARALGPDRPVYGLQ 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 1099 SPRPNGPMQTAANLDEVCEAHLATLLEQQPHGPYYLLGYSLGGTLAQGIAARLRARGEQVAFLGLLDTWPPETQNWQEKE 1178
Cdd:COG3319 635 APGLDGGEPPPASVEEMAARYVEAIRAVQPEGPYHLLGWSFGGLVAYEMARQLEAQGEEVALLVLLDSYAPGALARLDEA 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 1179 ----------ANGLDPEVLAEINRE------REAFLAAQQ-----GSTSTELFTTIEGNYADAVRLLTTAHSVPFDGKAT 1237
Cdd:COG3319 715 ellaallrdlARGVDLPLDAEELRAldpeerLARLLERLReaglpAGLDAERLRRLLRVFRANLRALRRYRPRPYDGPVL 794
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 16128569 1238 LFVAERTLQEG-MSPERAWSPWIA-ELDIYRQDCAHVDIISPGTFEKIGPIIRATLNR 1293
Cdd:COG3319 795 LFRAEEDPPGRaDDPALGWRPLVAgGLEVHDVPGDHFSMLREPHVAELAAALRAALAA 852
|
|
| D-ala-DACP-lig |
TIGR01734 |
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ... |
465-958 |
2.38e-62 |
|
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also called D-alanine-D-alanyl carrier protein ligase) which activates D-alanine as an adenylate via the reaction D-ala + ATP -> D-ala-AMP + PPi, and further catalyzes the condensation of the amino acid adenylate with the D-alanyl carrier protein (D-ala-ACP). The D-alanine is then further transferred to teichoic acid in the biosynthesis of lipoteichoic acid (LTA) and wall teichoic acid (WTA) in gram positive bacteria, both polysacchatides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273780 [Multi-domain] Cd Length: 502 Bit Score: 221.94 E-value: 2.38e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 465 AAKTPDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRL 544
Cdd:TIGR01734 10 AETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPVDTSIPSERI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 545 KMMLEDARPSLLITTDDQLPRFSDVPNLTSLCYNAPLTPQGsaPLQLSQP---HHTAYIIFTSGSTGRPKGVMVGQTAIV 621
Cdd:TIGR01734 90 EMIIEAAGPELVIHTAELSIDAVGTQIITLSALEQAETSGG--PVSFDHAvkgDDNYYIIYTSGSTGNPKGVQISHDNLV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 622 NRLLWMQNHYPLTGEDVVAQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPlamQQFFAEYG-------VTTTHFVP 694
Cdd:TIGR01734 168 SFTNWMLADFPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTLHCLDKDITNNF---KLLFEELPktglnvwVSTPSFVD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 695 smlaafVASLTPQTARQSCATLKQVFCSGEALPADLCREW-QQLTGAPLHNLYGPTEAAVDVSWYPAFGEELAQVrgSSV 773
Cdd:TIGR01734 245 ------MCLLDPNFNQENYPHLTHFLFCGEELPVKTAKALlERFPKATIYNTYGPTEATVAVTSVKITQEILDQY--PRL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 774 PIGYPVWNTGLRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIadpFAPGERMYRTGDVARwLDNGAVEYL 853
Cdd:TIGR01734 317 PIGFAKPDMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAFF---SHEGQPAYRTGDAGT-ITDGQLFYQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 854 GRSDDQLKIRGQRIELGEIDRVMQALPDVEQAVTHACVINQAAATggdarQLVGYLVSQsglPLD-------TSALQAQL 926
Cdd:TIGR01734 393 GRLDFQIKLHGYRIELEDIEFNLRQSSYIESAVVVPKYNKDHKVE-----YLIAAIVPE---TEDfekefqlTKAIKKEL 464
|
490 500 510
....*....|....*....|....*....|..
gi 16128569 927 RETLPPHMVPVVLLQLPQLPLSANGKLDRKAL 958
Cdd:TIGR01734 465 KKSLPAYMIPRKFIYRDQLPLTANGKIDRKAL 496
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
596-933 |
7.76e-61 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 212.15 E-value: 7.76e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 596 HTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTGEDVVAQKTPCSFDVSVWEFFWPFIAGAKLVMAEPeahRDP 675
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPK---FDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 676 LAMQQFFAEYGVTTTHFVPSMLAAFVAslTPQTARQSCATLKQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVDV 755
Cdd:cd04433 78 EAALELIEREKVTILLGVPTLLARLLK--APESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 756 SWYPAFGEElaqvrGSSVPIGYPVWNTGLRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFiadpfapGERM 835
Cdd:cd04433 156 ATGPPDDDA-----RKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD-------EDGW 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 836 YRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQavthACVINQAAATGGDArqLVGYLVSQSGL 915
Cdd:cd04433 224 YRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAE----AAVVGVPDPEWGER--VVAVVVLRPGA 297
|
330
....*....|....*...
gi 16128569 916 PLDTSALQAQLRETLPPH 933
Cdd:cd04433 298 DLDAEELRAHVRERLAPY 315
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
465-958 |
5.03e-60 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 215.14 E-value: 5.03e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 465 AAKTPDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRL 544
Cdd:PRK04813 12 AQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSPAERI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 545 KMMLEDARPSLLITTDDQLPRFSDVPNLTSLCYNAPLTPQGSAPL-QLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNR 623
Cdd:PRK04813 92 EMIIEVAKPSLIIATEELPLEILGIPVITLDELKDIFATGNPYDFdHAVKGDDNYYIIFTSGTTGKPKGVQISHDNLVSF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 624 LLWMQNHYPL-TGEDVVAQkTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPlamQQFFAEygVTTTHF-----VPS-- 695
Cdd:PRK04813 172 TNWMLEDFALpEGPQFLNQ-APYSFDLSVMDLYPTLASGGTLVALPKDMTANF---KQLFET--LPQLPInvwvsTPSfa 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 696 ----MLAAFVASLTPQtarqscatLKQ-VFCsGEALPAdlcREWQQLT----GAPLHNLYGPTEAAVDVSWYPAFGEELA 766
Cdd:PRK04813 246 dmclLDPSFNEEHLPN--------LTHfLFC-GEELPH---KTAKKLLerfpSATIYNTYGPTEATVAVTSIEITDEMLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 767 QVrgSSVPIGYPVWNTGLRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADpfaPGERMYRTGDVARwLD 846
Cdd:PRK04813 314 QY--KRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFTF---DGQPAYHTGDAGY-LE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 847 NGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQAVthACVINQaaatGGDARQLVGYLVSQSG-----LPLdTSA 921
Cdd:PRK04813 388 DGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAV--VVPYNK----DHKVQYLIAYVVPKEEdfereFEL-TKA 460
|
490 500 510
....*....|....*....|....*....|....*..
gi 16128569 922 LQAQLRETLPPHMVPVVLLQLPQLPLSANGKLDRKAL 958
Cdd:PRK04813 461 IKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| Thioesterase |
pfam00975 |
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ... |
1066-1287 |
1.12e-57 |
|
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.
Pssm-ID: 395776 [Multi-domain] Cd Length: 223 Bit Score: 198.77 E-value: 1.12e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 1066 PTLFCFHPASGFAWQFSVLSRYLDPQWSIIGIQSPRPNGPMQTAANLDEVCEAHLATLLEQQPHGPYYLLGYSLGGTLAQ 1145
Cdd:pfam00975 1 RPLFCFPPAGGSASSFRSLARRLPPPAEVLAVQYPGRGRGEPPLNSIEALADEYAEALRQIQPEGPYALFGHSMGGMLAF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 1146 GIAARLRARGEQVAFLGLLDTWPPETqNWQEKEANGLDPEVLAEINREREaflAAQQGSTSTELFTTIEGNYADAVRLLT 1225
Cdd:pfam00975 81 EVARRLERQGEAVRSLFLSDASAPHT-VRYEASRAPDDDEVVAEFTDEGG---TPEELLEDEELLSMLLPALRADYRALE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128569 1226 TAHSVPFDG-KATLFVAERTLQEGMS--PERAWSPWIAELDIYRQDCAHVDIIS--PGTFEKIGPII 1287
Cdd:pfam00975 157 SYSCPPLDAqSATLFYGSDDPLHDADdlAEWVRDHTPGEFDVHVFDGDHFYLIEhlEAVLEIIEAKL 223
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
465-933 |
7.88e-57 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 207.27 E-value: 7.88e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 465 AAKTPDAPAL-----ADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGY 539
Cdd:COG0365 19 AEGRGDKVALiwegeDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 540 -PDDrLKMMLEDARPSLLITTDDQLPRFSDVP----------NLTSL-------CYNAPLTPQGSAPL-----QLSQPH- 595
Cdd:COG0365 99 gAEA-LADRIEDAEAKVLITADGGLRGGKVIDlkekvdealeELPSLehvivvgRTGADVPMEGDLDWdellaAASAEFe 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 596 -------HTAYIIFTSGSTGRPKGVMVGQTAIVNRLLW-MQNHYPLTGEDVVAQKTPCSFDVSVW-EFFWPFIAGAKLVM 666
Cdd:COG0365 178 peptdadDPLFILYTSGTTGKPKGVVHTHGGYLVHAATtAKYVLDLKPGDVFWCTADIGWATGHSyIVYGPLLNGATVVL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 667 AE-PEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPQTARQSCATLKQVFCSGEALPADLCREWQQLTGAPLHNL 745
Cdd:COG0365 258 YEgRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDLSSLRLLGSAGEPLNPEVWEWWYEAVGVPIVDG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 746 YGPTEA-AVDVSWYPAfgeeLAQVRGSsvpIGYPVWNTGLRILDAMMHPVPPGVAGDLYLTG--IQLAQGYLGRPDLTAS 822
Cdd:COG0365 338 WGQTETgGIFISNLPG----LPVKPGS---MGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGpwPGMFRGYWNDPERYRE 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 823 RFiadpFAPGERMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQAVthacVINQAAATGGDA 902
Cdd:COG0365 411 TY----FGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAA----VVGVPDEIRGQV 482
|
490 500 510
....*....|....*....|....*....|....
gi 16128569 903 rqLVGYLVSQSGLPLD---TSALQAQLRETLPPH 933
Cdd:COG0365 483 --VKAFVVLKPGVEPSdelAKELQAHVREELGPY 514
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
292-1043 |
5.95e-56 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 213.77 E-value: 5.95e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 292 NVLPLGIHIAAQETLPELATRLAAQLKKMRRHQRYDAEQIVRDSGRAAGDEPLfgPVL-NIKVFDYQldipdvQAQTHTL 370
Cdd:TIGR03443 80 RPFVLRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAKKLERT--PPLfRLAFQDAP------DNQQTTY 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 371 ATGPVNDLELALFPDvHGDLSIEILANKQRYDEPTLIQHAERLKMLIAQFAADPALLCGDVDIMLPGEYAQLaqlnatqv 450
Cdd:TIGR03443 152 STGSTTDLTVFLTPS-SPELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPIGKVSLITPSQKSLL-------- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 451 eiPETT-----------LSALVAEQAAKTPD---------APALADARYLFSYREMREQVVALANLLRERGVKPGDSVAV 510
Cdd:TIGR03443 223 --PDPTkdldwsgfrgaIHDIFADNAEKHPDrtcvvetpsFLDPSSKTRSFTYKQINEASNILAHYLLKTGIKRGDVVMI 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 511 ALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLIT--------------TDDQLPRFSDVPnltSLC 576
Cdd:TIGR03443 301 YAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLSVAKPRALIViekagtldqlvrdyIDKELELRTEIP---ALA 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 577 YNAPLTPQGSAP-------LQLSQ------------PHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTGED 637
Cdd:TIGR03443 378 LQDDGSLVGGSLeggetdvLAPYQalkdtptgvvvgPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFGLSEND 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 638 VVAQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPQTArqscaTLK 717
Cdd:TIGR03443 458 KFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTADDIGTPGRLAEWMAKYGATVTHLTPAMGQLLSAQATTPIP-----SLH 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 718 QVFCSGEALPADLCREWQQLtgAP---LHNLYGPTEAAVDVSWY--------PAFGEELAQVrgssVPIGYPVWNTGLRI 786
Cdd:TIGR03443 533 HAFFVGDILTKRDCLRLQTL--AEnvcIVNMYGTTETQRAVSYFeipsrssdSTFLKNLKDV----MPAGKGMKNVQLLV 606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 787 LDAMMHPVPPGVA--GDLYLTGIQLAQGYLGRPDLTASRFI----ADP------------------FAPGERMYRTGDVA 842
Cdd:TIGR03443 607 VNRNDRTQTCGVGevGEIYVRAGGLAEGYLGLPELNAEKFVnnwfVDPshwidldkennkperefwLGPRDRLYRTGDLG 686
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 843 RWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQAVT-------------------------HACVINQAAA 897
Cdd:TIGR03443 687 RYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTlvrrdkdeeptlvsyivpqdksdelEEFKSEVDDE 766
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 898 TGGDarQLVGYLVSQSGLPLDtsaLQAQLRETLPPHMVPVVLLQLPQLPLSANGKLDRKALPLP---ELKAQAPGRAPKA 974
Cdd:TIGR03443 767 ESSD--PVVKGLIKYRKLIKD---IREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPdtaQLAAVAKNRSASA 841
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128569 975 GSETI------IAAAFSSLL--GCDVQDADADFFALGGHSLLAMKLAAQLSRQVARQVTPGQVMVASTVAKLATIID 1043
Cdd:TIGR03443 842 ADEEFtetereIRDLWLELLpnRPATISPDDSFFDLGGHSILATRMIFELRKKLNVELPLGLIFKSPTIKGFAKEVD 918
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
457-958 |
2.48e-51 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 188.54 E-value: 2.48e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 457 LSALVAEQAAKTPDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLD 536
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 537 TGYPDDRLKMMLEDARPSLLITTDDqlprFSDVpnltslcYNAPLTPQGSAPLqlsQPHHTAYIIFTSGSTGRPKGVMVG 616
Cdd:cd05936 81 PLYTPRELEHILNDSGAKALIVAVS----FTDL-------LAAGAPLGERVAL---TPEDVAVLQYTSGTTGVPKGAMLT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 617 QTAIVNRLLWMQNHYP--LTGEDVVAQKTPC--SFDVSVwEFFWPFIAGAKLVMaEPEAhRDPLAMQQfFAEYGVTTTHF 692
Cdd:cd05936 147 HRNLVANALQIKAWLEdlLEGDDVVLAALPLfhVFGLTV-ALLLPLALGATIVL-IPRF-RPIGVLKE-IRKHRVTIFPG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 693 VPSMLAAFVASLTPQTARQScaTLKQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVDVSWYPAFGEelaQVRGSs 772
Cdd:cd05936 223 VPTMYIALLNAPEFKKRDFS--SLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSPVVAVNPLDGP---RKPGS- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 773 vpIGYPVWNTGLRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermyRTGDVARWLDNGAVEY 852
Cdd:cd05936 297 --IGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL-------RTGDIGYMDEDGYFFI 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 853 LGRSDDQLKIRGQRIELGEIDRVMQALPDVEQAVthacVINQAAATGGDArqLVGYLVSQSGLPLDTSALQAQLRETLPP 932
Cdd:cd05936 368 VDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAA----VVGVPDPYSGEA--VKAFVVLKEGASLTEEEIIAFCREQLAG 441
|
490 500
....*....|....*....|....*.
gi 16128569 933 HMVPVVLLQLPQLPLSANGKLDRKAL 958
Cdd:cd05936 442 YKVPRQVEFRDELPKSAVGKILRREL 467
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
481-961 |
2.66e-49 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 184.26 E-value: 2.66e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 481 FSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTD 560
Cdd:cd17647 21 FTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPRGLIVIR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 561 DqlprfSDVpnltslcynapltpqgsaplqLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTGEDVVA 640
Cdd:cd17647 101 A-----AGV---------------------VVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKFT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 641 QKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPQTArqscaTLKQVF 720
Cdd:cd17647 155 MLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAMGQLLTAQATTPFP-----KLHHAF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 721 CSGEALPADLCREWQQLT-GAPLHNLYGPTEAAVDVSWY--------PAFGEELAQVrgssVPIGYPVWNTGLRILDAMM 791
Cdd:cd17647 230 FVGDILTKRDCLRLQTLAeNVRIVNMYGTTETQRAVSYFevpsrssdPTFLKNLKDV----MPAGRGMLNVQLLVVNRND 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 792 HPVPPGVA--GDLYLTGIQLAQGYLGRPDLTASRFI----ADP------------------FAPGERMYRTGDVARWLDN 847
Cdd:cd17647 306 RTQICGIGevGEIYVRAGGLAEGYRGLPELNKEKFVnnwfVEPdhwnyldkdnnepwrqfwLGPRDRLYRTGDLGRYLPN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 848 GAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQAVThaCVINQAaatgGDARQLVGYLVSQSGLPLDTSA------ 921
Cdd:cd17647 386 GDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENIT--LVRRDK----DEEPTLVSYIVPRFDKPDDESFaqedvp 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128569 922 ---------------------LQAQLRETLPPHMVPVVLLQLPQLPLSANGKLDRKALPLP 961
Cdd:cd17647 460 kevstdpivkgligyrklikdIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
465-930 |
5.85e-45 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 168.94 E-value: 5.85e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 465 AAKTPDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSV-FLTLALhAIVEAGAAWLPLDTGYPDDR 543
Cdd:cd17631 5 ARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPeFLELLF-AAARLGAVFVPLNFRLTPPE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 544 LKMMLEDARPSLLIttDDqlprfsdvpnltslcynapltpqgsaplqlsqphhTAYIIFTSGSTGRPKGVMVGQTAivnr 623
Cdd:cd17631 84 VAYILADSGAKVLF--DD-----------------------------------LALLMYTSGTTGRPKGAMLTHRN---- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 624 LLWM-QNH---YPLTGEDVVAQKTPCsFDVSVWEFFWPFI--AGAKLVMaepEAHRDPLAMQQFFAEYGVTTTHFVPSML 697
Cdd:cd17631 123 LLWNaVNAlaaLDLGPDDVLLVVAPL-FHIGGLGVFTLPTllRGGTVVI---LRKFDPETVLDLIERHRVTSFFLVPTMI 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 698 AAFVASltPQTARQSCATLKQVFCSGEALPADLCREWQqLTGAPLHNLYGPTEAAVDVSWYPAfgEELAQVRGSsvpIGY 777
Cdd:cd17631 199 QALLQH--PRFATTDLSSLRAVIYGGAPMPERLLRALQ-ARGVKFVQGYGMTETSPGVTFLSP--EDHRRKLGS---AGR 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 778 PVWNTGLRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASrFIADPFapgermYRTGDVARWLDNGAVEYLGRSD 857
Cdd:cd17631 271 PVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAA-AFRDGW------FHTGDLGRLDEDGYLYIVDRKK 343
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128569 858 DQLKIRGQRIELGEIDRVMQALPDVEQAVthacVINQAAATGGDARQLVgyLVSQSGLPLDTSALQAQLRETL 930
Cdd:cd17631 344 DMIISGGENVYPAEVEDVLYEHPAVAEVA----VIGVPDEKWGEAVVAV--VVPRPGAELDEDELIAHCRERL 410
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
469-958 |
1.06e-44 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 168.80 E-value: 1.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 469 PDAPALAD----ARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRL 544
Cdd:cd17654 1 PDRPALIIdqttSDTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 545 KMMLEDARPSLLITTDDQLprfsdvpnltslcyNAPLTPQGSA-PLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNR 623
Cdd:cd17654 81 LTVMKKCHVSYLLQNKELD--------------NAPLSFTPEHrHFNIRTDECLAYVIHTSGTTGTPKIVAVPHKCILPN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 624 LLWMQNHYPLTGEDVVAQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQ-FFAEYGVTTTHFVPSMLAAFVA 702
Cdd:cd17654 147 IQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADiLFKRHRITVLQATPTLFRRFGS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 703 SLTPQTARQSCATLKQVFCSGEALPAD-LCREW-QQLTGAPLHNLYGPTEAAVDVSWYpafgeeLAQVRGSSVPIGYPVW 780
Cdd:cd17654 227 QSIKSTVLSATSSLRVLALGGEPFPSLvILSSWrGKGNRTRIFNIYGITEVSCWALAY------KVPEEDSPVQLGSPLL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 781 NTGLRILDAMMHPvppgVAGDLYLTGIQLA---QGYLGRPDLTasrfiadpfapgerMYRTGDVARwLDNGAVEYLGRSD 857
Cdd:cd17654 301 GTVIEVRDQNGSE----GTGQVFLGGLNRVcilDDEVTVPKGT--------------MRATGDFVT-VKDGELFFLGRKD 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 858 DQLKIRGQRIELGEIDRVMQALPDVEQAVThacvinqaaaTGGDARQLVGYLVSQsglPLDTSALQAQLRETLPPHMVPV 937
Cdd:cd17654 362 SQIKRRGKRINLDLIQQVIESCLGVESCAV----------TLSDQQRLIAFIVGE---SSSSRIHKELQLTLLSSHAIPD 428
|
490 500
....*....|....*....|.
gi 16128569 938 VLLQLPQLPLSANGKLDRKAL 958
Cdd:cd17654 429 TFVQIDKLPLTSHGKVDKSEL 449
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
481-902 |
2.31e-44 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 168.55 E-value: 2.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 481 FSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTD 560
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 561 DQLPRFS-----------------------DVPNLTSLCYNAPLTPQgsaPLQLSQPH-HTAYIIFTSGSTGRPKGVMVG 616
Cdd:cd05911 91 DGLEKVKeaakelgpkdkiivlddkpdgvlSIEDLLSPTLGEEDEDL---PPPLKDGKdDTAAILYSSGTTGLPKGVCLS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 617 QTAIVNRLLWMQNHYPLTG--EDVVaqktpcsfdVSVWEFFWpfIAGAKLVMAEPeAHRDPL-AMQQFFAE--------Y 685
Cdd:cd05911 168 HRNLIANLSQVQTFLYGNDgsNDVI---------LGFLPLYH--IYGLFTTLASL-LNGATViIMPKFDSElfldliekY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 686 GVTTTHFVPSMLAAFVASltPQTARQSCATLKQVFCSGEALPADLCREWQQL-TGAPLHNLYGPTEAAVDVSWYPAFGEe 764
Cdd:cd05911 236 KITFLYLVPPIAAALAKS--PLLDKYDLSSLRVILSGGAPLSKELQELLAKRfPNATIKQGYGMTETGGILTVNPDGDD- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 765 laqVRGSSvpiGYPVWNTGLRILD-AMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermYRTGDVAR 843
Cdd:cd05911 313 ---KPGSV---GRLLPNVEAKIVDdDGKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW------LHTGDIGY 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 16128569 844 WLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVEqavtHACVINQAAATGGDA 902
Cdd:cd05911 381 FDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVA----DAAVIGIPDEVSGEL 435
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
481-926 |
1.77e-42 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 161.78 E-value: 1.77e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 481 FSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTD 560
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 561 dqlpRFsdvpnltslcynapltpQGSAPLQlsQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTGEDVVA 640
Cdd:cd05903 82 ----RF-----------------RQFDPAA--MPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 641 QKTPCS-FDVSVWEFFWPFIAGAKLVMAEPeahRDPLAMQQFFAEYGVTTthfvpsMLAA--FVASL--TPQTARQSCAT 715
Cdd:cd05903 139 VASPMAhQTGFVYGFTLPLLLGAPVVLQDI---WDPDKALALMREHGVTF------MMGAtpFLTDLlnAVEEAGEPLSR 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 716 LKQVFCSGEALPADLCREWQQLTGAPLHNLYGPTE--AAVDVSwypafgeELAQVRGSSVPIGYPVWNTGLRILDAMMHP 793
Cdd:cd05903 210 LRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTEcpGAVTSI-------TPAPEDRRLYTDGRPLPGVEIKVVDDTGAT 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 794 VPPGVAGDLYLTGIQLAQGYLGRPDLTASrfiadpfAPGERMYRTGDVARWLDNGAVEYLGRSDDqLKIR-GQRIELGEI 872
Cdd:cd05903 283 LAPGVEGELLSRGPSVFLGYLDRPDLTAD-------AAPEGWFRTGDLARLDEDGYLRITGRSKD-IIIRgGENIPVLEV 354
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 16128569 873 DRVMQALPDVEQavthACVINQAaatggDAR---QLVGYLVSQSGLPLDTSALQAQL 926
Cdd:cd05903 355 EDLLLGHPGVIE----AAVVALP-----DERlgeRACAVVVTKSGALLTFDELVAYL 402
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
480-934 |
2.06e-41 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 158.22 E-value: 2.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 480 LFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITT 559
Cdd:cd05934 3 RWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 560 ddqlprfsdvpnltslcynapltpqgsaplqlsqphhTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTGEDVV 639
Cdd:cd05934 83 -------------------------------------PASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVY 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 640 AQKTPCSF-DVSVWEFFWPFIAGAKLVMaepeahRDPLAMQQFFA---EYGVTTTHFVPSMLAAFVAslTPQTARQSCAT 715
Cdd:cd05934 126 LTVLPLFHiNAQAVSVLAALSVGATLVL------LPRFSASRFWSdvrRYGATVTNYLGAMLSYLLA--QPPSPDDRAHR 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 716 LKQVFCSgeALPADLCREWQQLTGAPLHNLYGPTEAAVDVswypafgeeLAQVRGSSVP--IGYPVWNTGLRILDAMMHP 793
Cdd:cd05934 198 LRAAYGA--PNPPELHEEFEERFGVRLLEGYGMTETIVGV---------IGPRDEPRRPgsIGRPAPGYEVRIVDDDGQE 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 794 VPPGVAGDLYLTGIQ---LAQGYLGRPDLTASRfiadpFAPGerMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELG 870
Cdd:cd05934 267 LPAGEPGELVIRGLRgwgFFKGYYNMPEATAEA-----MRNG--WFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSA 339
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128569 871 EIDRVMQALPDVEQAVthacVINQAAATGGDarQLVGYLVSQSGLPLDTSALQAQLRETLPPHM 934
Cdd:cd05934 340 EVERAILRHPAVREAA----VVAVPDEVGED--EVKAVVVLRPGETLDPEELFAFCEGQLAYFK 397
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
456-886 |
1.25e-40 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 158.43 E-value: 1.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 456 TLSALVAEQAAKTPDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRS-VFLTlALHAIVEAGAAWLP 534
Cdd:PRK06187 7 TIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNShEYLE-AYFAVPKIGAVLHP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 535 LDTGYPDDRLKMMLEDARPSLLITTDDQLPRFSDV-PNLTSL--------CYNAPLTPQG--------SAPLQLSQPH-- 595
Cdd:PRK06187 86 INIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAIlPQLPTVrtvivegdGPAAPLAPEVgeyeellaAASDTFDFPDid 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 596 -HTAYIIF-TSGSTGRPKGVM------VGQTAIVNRllWMQnhypLTGEDVVAQKTPCsFDVSVWEffWPFIA---GAKL 664
Cdd:PRK06187 166 eNDAAAMLyTSGTTGHPKGVVlshrnlFLHSLAVCA--WLK----LSRDDVYLVIVPM-FHVHAWG--LPYLAlmaGAKQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 665 VMaepeAHR-DPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPQTARQScaTLKQVFCSGEALPADLCREWQQLTGAPLH 743
Cdd:PRK06187 237 VI----PRRfDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFS--SLRLVIYGGAALPPALLREFKEKFGIDLV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 744 NLYGPTEAA--VDVSWYPAFGEELAQVRGSSvpiGYPVWNTGLRILDAMMHPVPP--GVAGDLYLTGIQLAQGYLGRPDL 819
Cdd:PRK06187 311 QGYGMTETSpvVSVLPPEDQLPGQWTKRRSA---GRPLPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLMQGYWNRPEA 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128569 820 TASRFIADpfapgerMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDV-EQAV 886
Cdd:PRK06187 388 TAETIDGG-------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVaEVAV 448
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
472-958 |
3.03e-40 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 155.31 E-value: 3.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 472 PALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDA 551
Cdd:cd05919 2 TAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 552 RPSLLITTDDQLprfsdvpnltslcynapltpqgsaplqlsqphhtAYIIFTSGSTGRPKGVMvgqTAIVNRLL----WM 627
Cdd:cd05919 82 EARLVVTSADDI----------------------------------AYLLYSSGTTGPPKGVM---HAHRDPLLfadaMA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 628 QNHYPLTGEDVVAQKTPCSFDVSVWEFFW-PFIAGAKLVMAEpeAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASltP 706
Cdd:cd05919 125 REALGLTPGDRVFSSAKMFFGYGLGNSLWfPLAVGASAVLNP--GWPTAERVLATLARFRPTVLYGVPTFYANLLDS--C 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 707 QTARQSCATLKQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAA-VDVSWYPAfgeelaQVR-GSSvpiGYPVWNTGL 784
Cdd:cd05919 201 AGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGhIFLSNRPG------AWRlGST---GRPVPGYEI 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 785 RILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIadpfapgERMYRTGDVARWLDNGAVEYLGRSDDQLKIRG 864
Cdd:cd05919 272 RLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFN-------GGWYRTGDKFCRDADGWYTHAGRADDMLKVGG 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 865 QRIELGEIDRVMQALPDVEQAVTHACvinqaaATGGDARQLVGYLVSQSGLPLDTS---ALQAQLRETLPPHMVPVVLLQ 941
Cdd:cd05919 345 QWVSPVEVESLIIQHPAVAEAAVVAV------PESTGLSRLTAFVVLKSPAAPQESlarDIHRHLLERLSAHKVPRRIAF 418
|
490
....*....|....*..
gi 16128569 942 LPQLPLSANGKLDRKAL 958
Cdd:cd05919 419 VDELPRTATGKLQRFKL 435
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
469-890 |
6.69e-40 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 155.55 E-value: 6.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 469 PDAPALA--DARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKM 546
Cdd:cd05926 1 PDAPALVvpGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 547 MLEDARPSLLITTDDQL-----------PRFSDVPNLTSLCYNAP---------LTPQGSAPLQLSQPHHTAYIIFTSGS 606
Cdd:cd05926 81 YLADLGSKLVLTPKGELgpasraasklgLAILELALDVGVLIRAPsaeslsnllADKKNAKSEGVPLPDDLALILHTSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 607 TGRPKGVMVGQTAIVNRLLWMQNHYPLTGEDVVAQKTPCsFDVS--VWEFFWPFIAGAKLVMAepeAHRDPLAMQQFFAE 684
Cdd:cd05926 161 TGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPL-FHVHglVASLLSTLAAGGSVVLP---PRFSASTFWPDVRD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 685 YGVTTTHFVPSMLAAFVASLTPQTaRQSCATLKQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVDVSWYPAfgeE 764
Cdd:cd05926 237 YNATWYTAVPTIHQILLNRPEPNP-ESPPPKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAHQMTSNPL---P 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 765 LAQVRGSSVPIGYpvwNTGLRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermYRTGDVARW 844
Cdd:cd05926 313 PGPRKPGSVGKPV---GVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW------FRTGDLGYL 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 16128569 845 LDNGaveYL---GRSDDQLKIRGQRIELGEIDRVMQALPDVEQAVTHAC 890
Cdd:cd05926 384 DADG---YLfltGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGV 429
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
469-958 |
1.75e-38 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 151.75 E-value: 1.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 469 PDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSV-FLTLALHAIvEAGAAWLPLDTGYPDDRLKMM 547
Cdd:cd05959 18 GDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVdFPTAFLGAI-RAGIVPVPVNTLLTPDDYAYY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 548 LEDARPSLLITTDDQLPRFSDVPNL-------------------TSLCYNAPLTPQGSAPLQLSQPHHTAYIIFTSGSTG 608
Cdd:cd05959 97 LEDSRARVVVVSGELAPVLAAALTKsehtlvvlivsggagpeagALLLAELVAAEAEQLKPAATHADDPAFWLYSSGSTG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 609 RPKGVMVGQTAIVnrllWMQNHYP-----LTGEDVVaqktpcsFDVSVWEF--------FWPFIAGAK-LVMAE-PEAHR 673
Cdd:cd05959 177 RPKGVVHLHADIY----WTAELYArnvlgIREDDVC-------FSAAKLFFayglgnslTFPLSVGATtVLMPErPTPAA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 674 DPLAMQQ-----FFAeygvttthfVPSMLAAFVASLTPQTARQScaTLKQVFCSGEALPADLCREWQQLTGAPLHNLYGP 748
Cdd:cd05959 246 VFKRIRRyrptvFFG---------VPTLYAAMLAAPNLPSRDLS--SLRLCVSAGEALPAEVGERWKARFGLDILDGIGS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 749 TEAA-VDVSWYPafgeelAQVR-GSSvpiGYPVWNTGLRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIa 826
Cdd:cd05959 315 TEMLhIFLSNRP------GRVRyGTT---GKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 827 dpfapGErMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDV-EQAVThacvinqAAATGGDARQL 905
Cdd:cd05959 385 -----GE-WTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVlEAAVV-------GVEDEDGLTKP 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 16128569 906 VGYLVSQSGLPlDTSALQAQLRE----TLPPHMVPVVLLQLPQLPLSANGKLDRKAL 958
Cdd:cd05959 452 KAFVVLRPGYE-DSEALEEELKEfvkdRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
456-933 |
4.06e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 151.23 E-value: 4.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 456 TLSALVAEQAAKTPDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPL 535
Cdd:PRK07788 50 PFAGLVAHAARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 536 DTGYPDDRLKMMLEDARPSLLITTDDQLPRFS----DVPNLTSLCYNA-PLTPQGSAPLQLSQ-------------PHHT 597
Cdd:PRK07788 130 NTGFSGPQLAEVAAREGVKALVYDDEFTDLLSalppDLGRLRAWGGNPdDDEPSGSTDETLDDliagsstaplpkpPKPG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 598 AYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTGEDVVAQKTPC--SFDVSVWEFFWPFiaGAKLVMaepeaHR-- 673
Cdd:PRK07788 210 GIVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMfhATGWAHLTLAMAL--GSTVVL-----RRrf 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 674 DPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPQTARQSCATLKQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAV 753
Cdd:PRK07788 283 DPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYDTSSLKIIFVSGSALSPELATRALEAFGPVLYNLYGSTEVAF 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 754 DVSWYPafgEELAQVRGSsvpIGYPVWNTGLRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGrpdlTASRFIADPfapge 833
Cdd:PRK07788 363 ATIATP---EDLAEAPGT---VGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTD----GRDKQIIDG----- 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 834 rMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVEqavthacvinQAAATGGD-----ARqLVGY 908
Cdd:PRK07788 428 -LLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVV----------EAAVIGVDdeefgQR-LRAF 495
|
490 500
....*....|....*....|....*
gi 16128569 909 LVSQSGLPLDTSALQAQLRETLPPH 933
Cdd:PRK07788 496 VVKAPGAALDEDAIKDYVRDNLARY 520
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
470-933 |
1.14e-36 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 144.74 E-value: 1.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 470 DAPALADARYLFSYREMREQVVALAN-LLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMML 548
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANrLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 549 EDARPSLLIttDDqlprfsdvpnltslcynapltpqgsaplqlsqphhtAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQ 628
Cdd:cd05941 81 TDSEPSLVL--DP------------------------------------ALILYTSGTTGRPKGVVLTHANLAANVRALV 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 629 NHYPLTGEDVVAQKTPCsFDVS--VWEFFWPFIAGAKLVM------AEPEAHRDPLAMQQFFAeygvttthfVPSM---- 696
Cdd:cd05941 123 DAWRWTEDDVLLHVLPL-HHVHglVNALLCPLFAGASVEFlpkfdpKEVAISRLMPSITVFMG---------VPTIytrl 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 697 LAAFVASLT-PQTARQSCATLKQVFCSGEA-LPADLCREWQQLTGAPLHNLYGPTEAAVDVSwYPAFGEELAqvrGSsvp 774
Cdd:cd05941 193 LQYYEAHFTdPQFARAAAAERLRLMVSGSAaLPVPTLEEWEAITGHTLLERYGMTEIGMALS-NPLDGERRP---GT--- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 775 IGYPVWNTGLRILD-AMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermYRTGDVARWLDNGAVEYL 853
Cdd:cd05941 266 VGMPLPGVQARIVDeETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW------FKTGDLGVVDEDGYYWIL 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 854 GR-SDDQLKIRGQRIELGEIDRVMQALPDveqaVTHACVINQAAATGGDArqLVGYLVSQSGL-PLDTSALQAQLRETLP 931
Cdd:cd05941 340 GRsSVDIIKSGGYKVSALEIERVLLAHPG----VSECAVIGVPDPDWGER--VVAVVVLRAGAaALSLEELKEWAKQRLA 413
|
..
gi 16128569 932 PH 933
Cdd:cd05941 414 PY 415
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
490-958 |
7.50e-35 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 139.88 E-value: 7.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 490 VVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAW----LPLDTGYPDDRLKMMLEDARPSLLIT------- 558
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLglvfVPLNPTLKESVLRYLVADAGGRIVLAdagaadr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 559 TDDQLPRFSDvpNLTSLCYNAPLTPQGSAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTGEDV 638
Cdd:cd05922 83 LRDALPASPD--PGTVLDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 639 VAQKTPCSFDVSVWEFFWPFIAGAKLVMAEpeAHRDPLAMQQFFAEYGVTTTHFVPSmLAAFVASLTPQTArqSCATLKQ 718
Cdd:cd05922 161 ALTVLPLSYDYGLSVLNTHLLRGATLVLTN--DGVLDDAFWEDLREHGATGLAGVPS-TYAMLTRLGFDPA--KLPSLRY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 719 VFCSGEALPADLCREWQQL-TGAPLHNLYGPTEAAVDVSWYPAfgEELAQVRGSsvpIGYPVWNTGLRILDAMMHPVPPG 797
Cdd:cd05922 236 LTQAGGRLPQETIARLRELlPGAQVYVMYGQTEATRRMTYLPP--ERILEKPGS---IGLAIPGGEFEILDDDGTPTPPG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 798 VAGDLYLTGIQLAQGYLGRPdltasRFIADPFAPGERMYrTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIdrvmq 877
Cdd:cd05922 311 EPGEIVHRGPNVMKGYWNDP-----PYRRKEGRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEI----- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 878 alpdvEQAVTHACVINQAAATGGD---ARQLVgyLVSQSGLPLDTSALQAQLRETLPPHMVPVVLLQLPQLPLSANGKLD 954
Cdd:cd05922 380 -----EAAARSIGLIIEAAAVGLPdplGEKLA--LFVTAPDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVD 452
|
....
gi 16128569 955 RKAL 958
Cdd:cd05922 453 YAAL 456
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
481-887 |
3.31e-34 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 137.08 E-value: 3.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 481 FSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTD 560
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 561 DQlprfsdvpnltslcynapltpqgsaplqlsqphhTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTGEDVVA 640
Cdd:cd05972 81 ED----------------------------------PALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIHW 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 641 QKTPCSFDVSVW-EFFWPFIAGAKLVMAEpEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPQTARqscATLKQV 719
Cdd:cd05972 127 NIADPGWAKGAWsSFFGPWLLGATVFVYE-GPRFDAERILELLERYGVTSFCGPPTAYRMLIKQDLSSYKF---SHLRLV 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 720 FCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVDVSWYPAfgeelAQVRGSSvpIGYPVWNTGLRILDAMMHPVPPGVA 799
Cdd:cd05972 203 VSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPD-----MPVKPGS--MGRPTPGYDVAIIDDDGRELPPGEE 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 800 GDL--YLTGIQLAQGYLGRPDLTASRFIADpfapgerMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQ 877
Cdd:cd05972 276 GDIaiKLPPPGLFLGYVGDPEKTEASIRGD-------YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALL 348
|
410
....*....|.
gi 16128569 878 ALPDV-EQAVT 887
Cdd:cd05972 349 EHPAVaEAAVV 359
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
481-928 |
4.91e-34 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 139.63 E-value: 4.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 481 FSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTD 560
Cdd:cd17634 85 ISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITAD 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 561 DQLPRFSDVPNLTSLcyNAPLTPQGSAPLQL---------------------------SQPHHTA--------YIIFTSG 605
Cdd:cd17634 165 GGVRAGRSVPLKKNV--DDALNPNVTSVEHVivlkrtgsdidwqegrdlwwrdliakaSPEHQPEamnaedplFILYTSG 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 606 STGRPKGVMVGQTAIVNRLLW-MQNHYPLTGEDVVAqktpCSFDVS-----VWEFFWPFIAGAKLVMAE--PEaHRDPLA 677
Cdd:cd17634 243 TTGKPKGVLHTTGGYLVYAATtMKYVFDYGPGDIYW----CTADVGwvtghSYLLYGPLACGATTLLYEgvPN-WPTPAR 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 678 MQQFFAEYGVTTTHFVPSMLAAFVASLTPQTARQSCATLKQVFCSGEALPADLCR-EWQQLTGA--PLHNLYGPTEaavd 754
Cdd:cd17634 318 MWQVVDKHGVNILYTAPTAIRALMAAGDDAIEGTDRSSLRILGSVGEPINPEAYEwYWKKIGKEkcPVVDTWWQTE---- 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 755 VSWY---PAFGEELAQVRGSSVPI-GYPVwntglRILDAMMHPVPPGVAGDLYLTGI--QLAQGYLGRPDltasRFIADP 828
Cdd:cd17634 394 TGGFmitPLPGAIELKAGSATRPVfGVQP-----AVVDNEGHPQPGGTEGNLVITDPwpGQTRTLFGDHE----RFEQTY 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 829 FAPGERMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPdveqAVTHACVINQAAATGGDArqLVGY 908
Cdd:cd17634 465 FSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHP----KVAEAAVVGIPHAIKGQA--PYAY 538
|
490 500
....*....|....*....|
gi 16128569 909 LVSQSGLpLDTSALQAQLRE 928
Cdd:cd17634 539 VVLNHGV-EPSPELYAELRN 557
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
456-930 |
1.67e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 136.57 E-value: 1.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 456 TLSALVAEQAAKTPDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPL 535
Cdd:PRK07656 6 TLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 536 DTGYPDDRLKMMLEDARPSLLITTDDQLPRF----SDVPNLTSLCYNAPLTPQGSAPLQLS-----------------QP 594
Cdd:PRK07656 86 NTRYTADEAAYILARGDAKALFVLGLFLGVDysatTRLPALEHVVICETEEDDPHTEKMKTftdflaagdpaerapevDP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 595 HHTAYIIFTSGSTGRPKGVMV--GQT-----AIVNRLlwmqnhyPLTGEDVVAQKTPcsfdvsvweFF--------W--P 657
Cdd:PRK07656 166 DDVADILFTSGTTGRPKGAMLthRQLlsnaaDWAEYL-------GLTEGDRYLAANP---------FFhvfgykagVnaP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 658 FIAGAKLVmaePEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVAslTPQTARQSCATLKqVFCSGEA-LPADLCREWQQ 736
Cdd:PRK07656 230 LMRGATIL---PLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQ--HPDRSAEDLSSLR-LAVTGAAsMPVALLERFES 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 737 -------LTGaplhnlYGPTEAAVDVSWYPAfGEELAQVRGSsvpIGYPVWNTGLRILDAMMHPVPPGVAGDLYLTGIQL 809
Cdd:PRK07656 304 elgvdivLTG------YGLSEASGVTTFNRL-DDDRKTVAGT---IGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNV 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 810 AQGYLGRPDLTASRFIADPFapgermYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQAVtha 889
Cdd:PRK07656 374 MKGYYDDPEATAAAIDADGW------LHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAA--- 444
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 16128569 890 cVInqaaatgG--DARQ-LVG--YLVSQSGLPLDTSALQAQLRETL 930
Cdd:PRK07656 445 -VI-------GvpDERLgEVGkaYVVLKPGAELTEEELIAYCREHL 482
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
456-886 |
2.92e-33 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 135.71 E-value: 2.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 456 TLSALVAEQAAKTPDAPALADAR--YLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWL 533
Cdd:cd05923 2 TVFEMLRRAASRAPDACAIADPArgLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 534 PLDTGYPDDRLKMMLEDARPSLLITTDDQLP------------RFSDVPNLTSLCYNAPLTPQgsaplQLSQPHHTAYII 601
Cdd:cd05923 82 LINPRLKAAELAELIERGEMTAAVIAVDAQVmdaifqsgvrvlALSDLVGLGEPESAGPLIED-----PPREPEQPAFVF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 602 FTSGSTGRPKGVMVGQTAIVNRLLWM--QNHYPLTGEDVVAQKTPCSFDVSVWEFFWPFIAGAKLVMaePEAHRDPLAMQ 679
Cdd:cd05923 157 YTSGTTGLPKGAVIPQRAAESRVLFMstQAGLRHGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYV--VVEEFDPADAL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 680 QFFAEYGVTTTHFVPSMLAAFVASLTPQTARQScaTLKQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAvdVSWY- 758
Cdd:cd05923 235 KLIEQERVTSLFATPTHLDALAAAAEFAGLKLS--SLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEAM--NSLYm 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 759 --PAFGEELAQVRGSSVPIgypvwntgLRILDAMMHPVPPGVAGDLYLTGIQLA--QGYLGRPDLTASRFIadpfapgER 834
Cdd:cd05923 311 rdARTGTEMRPGFFSEVRI--------VRIGGSPDEALANGEEGELIVAAAADAafTGYLNQPEATAKKLQ-------DG 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 16128569 835 MYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQAV 886
Cdd:cd05923 376 WYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVV 427
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
481-958 |
9.48e-33 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 132.94 E-value: 9.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 481 FSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTD 560
Cdd:cd05971 7 VTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTDG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 561 dqlprfSDVPnltslcynapltpqgsaplqlsqphhtAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQ---NHYPLTGeD 637
Cdd:cd05971 87 ------SDDP---------------------------ALIIYTSGTTGPPKGALHAHRVLLGHLPGVQfpfNLFPRDG-D 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 638 VVAqkTPCS-------FDVSVWEFFWpfiaGAKLVmaepeAHR----DPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTP 706
Cdd:cd05971 133 LYW--TPADwawigglLDVLLPSLYF----GVPVL-----AHRmtkfDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQ 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 707 QTARQscATLKQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVDVSWYPAfgeeLAQVRGSSvpIGYPVWNTGLRI 786
Cdd:cd05971 202 LKHAQ--VKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLVIGNCSA----LFPIKPGS--MGKPIPGHRVAI 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 787 LDAMMHPVPPGVAGDLyltGIQLAQ-----GYLGRPDLTASRFIADPFapgermyRTGDVARWLDNGAVEYLGRSDDQLK 861
Cdd:cd05971 274 VDDNGTPLPPGEVGEI---AVELPDpvaflGYWNNPSATEKKMAGDWL-------LTGDLGRKDSDGYFWYVGRDDDVIT 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 862 IRGQRIELGEIDRVMQALPdveqAVTHACVINQAAATGGDarQLVGYLVSQSGLpLDTSALQAQLRE----TLPPHMVPV 937
Cdd:cd05971 344 SSGYRIGPAEIEECLLKHP----AVLMAAVVGIPDPIRGE--IVKAFVVLNPGE-TPSDALAREIQElvktRLAAHEYPR 416
|
490 500
....*....|....*....|.
gi 16128569 938 VLLQLPQLPLSANGKLDRKAL 958
Cdd:cd05971 417 EIEFVNELPRTATGKIRRREL 437
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
465-930 |
3.39e-32 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 132.69 E-value: 3.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 465 AAKTPDAPAL--ADARYLfSYREMREQVVALANLLRERGVKPGDSVAVALPRSVfLTLALH-AIVEAGAAWLPLDTGYPD 541
Cdd:PRK07514 12 AFADRDAPFIetPDGLRY-TYGDLDAASARLANLLVALGVKPGDRVAVQVEKSP-EALALYlATLRAGAVFLPLNTAYTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 542 DRLKMMLEDARPSLLITTDDQLPRFSDVPNLTSLCYNAPLTPQGSAPL-----QLSQPHHT--------AYIIFTSGSTG 608
Cdd:PRK07514 90 AELDYFIGDAEPALVVCDPANFAWLSKIAAAAGAPHVETLDADGTGSLleaaaAAPDDFETvprgaddlAAILYTSGTTG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 609 RPKGVMVGQTAIVNRLLWMQNHYPLTGEDV--------------VAqkTPCSfdvsvweffwpFIAGAKLVMA---EPEA 671
Cdd:PRK07514 170 RSKGAMLSHGNLLSNALTLVDYWRFTPDDVlihalpifhthglfVA--TNVA-----------LLAGASMIFLpkfDPDA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 672 HRDplAMQQFFAEYGVTTthFVPSMLAAfvasltPQTARQSCATLKqVFCSGEA-LPADLCREWQQLTGAPLHNLYGPTE 750
Cdd:PRK07514 237 VLA--LMPRATVMMGVPT--FYTRLLQE------PRLTREAAAHMR-LFISGSApLLAETHREFQERTGHAILERYGMTE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 751 AAVDVSwYPAFGEElaqvRGSSVpiGYPVWNTGLRILD-AMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPF 829
Cdd:PRK07514 306 TNMNTS-NPYDGER----RAGTV--GFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGF 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 830 apgermYRTGDVARWLDNGAVEYLGRSDDqLKIRG------QRIElGEIDrvmqALPDV-EQAvthacVINQAAATGGDA 902
Cdd:PRK07514 379 ------FITGDLGKIDERGYVHIVGRGKD-LIISGgynvypKEVE-GEID----ELPGVvESA-----VIGVPHPDFGEG 441
|
490 500
....*....|....*....|....*...
gi 16128569 903 rqLVGYLVSQSGLPLDTSALQAQLRETL 930
Cdd:PRK07514 442 --VTAVVVPKPGAALDEAAILAALKGRL 467
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
482-892 |
6.59e-32 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 130.29 E-value: 6.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 482 SYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTDD 561
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGSE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 562 QlprfSDVpnltslcynapltpqgsaplqlsqphhtAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTGEDVVAQ 641
Cdd:cd05935 83 L----DDL----------------------------ALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 642 KTPCsFDVS--VWEFFWPFIAGAKLVMAepeAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVAslTPQTARQSCATLKQV 719
Cdd:cd05935 131 CLPL-FHVTgfVGSLNTAVYVGGTYVLM---ARWDRETALELIEKYKVTFWTNIPTMLVDLLA--TPEFKTRDLSSLKVL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 720 FCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVDVSWYPafgeelaQVRGSSVPIGYPVWNTGLRILDA-MMHPVPPGV 798
Cdd:cd05935 205 TGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNP-------PLRPKLQCLGIP*FGVDARVIDIeTGRELPPNE 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 799 AGDLYLTGIQLAQGYLGRPDLTASRFIADpfaPGERMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQA 878
Cdd:cd05935 278 VGEIVVRGPQIFKGYWNRPEETEESFIEI---KGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYK 354
|
410
....*....|....
gi 16128569 879 LPdveqAVTHACVI 892
Cdd:cd05935 355 HP----AI*EVCVI 364
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
456-885 |
1.27e-30 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 128.63 E-value: 1.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 456 TLSALVAEQAAKTPDAPALADARYL------FSYREMREQVVALANLLRERGVKPGDSVAVALPRSV-FLTLALhAIVEA 528
Cdd:PRK13295 25 TINDDLDACVASCPDKTAVTAVRLGtgaprrFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWeFTVLYL-ACSRI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 529 GAAWLPLDTGYPDDRLKMMLEDARPSLLI---------------TTDDQLPRFSDV-------PN------LTSLCYNAP 580
Cdd:PRK13295 104 GAVLNPLMPIFRERELSFMLKHAESKVLVvpktfrgfdhaamarRLRPELPALRHVvvvggdgADsfeallITPAWEQEP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 581 LTPQGSAPLQLSqPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTGEDVVAQKTPCSFDVS-VWEFFWPFI 659
Cdd:PRK13295 184 DAPAILARLRPG-PDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGfMYGLMMPVM 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 660 AGAKLVMAEPeahRDPLAMQQFFAEYGVTTThfvpsMLAA-FVASLT--PQTARQSCATLKQVFCSGEALPADLCREWQQ 736
Cdd:PRK13295 263 LGATAVLQDI---WDPARAAELIRTEGVTFT-----MASTpFLTDLTraVKESGRPVSSLRTFLCAGAPIPGALVERARA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 737 LTGAPLHNLYGPTEAAVDVSWYPAFGEELAQVRGssvpiGYPVWNTGLRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGR 816
Cdd:PRK13295 335 ALGAKIVSAWGMTENGAVTLTKLDDPDERASTTD-----GCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKR 409
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 817 PDLTASRFiadpfapgERMYRTGDVARWLDNGAVEYLGRSDDQLkIRG-QRIELGEIDRVMQALPDVEQA 885
Cdd:PRK13295 410 PQLNGTDA--------DGWFDTGDLARIDADGYIRISGRSKDVI-IRGgENIPVVEIEALLYRHPAIAQV 470
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
479-930 |
2.09e-30 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 127.78 E-value: 2.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 479 YLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDD-------RLKMMLEDA 551
Cdd:cd05906 38 EFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPTYDepnarlrKLRHIWQLL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 552 RPSLLITTDDQLPRFSDVPNLTSLCYNAPLT------PQGSAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLL 625
Cdd:cd05906 118 GSPVVLTDAELVAEFAGLETLSGLPGIRVLSieelldTAADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 626 WMQNHYPLTGEDVVAQKTPCSFDVSVWEF-FWPFIAGAKLVMAEPEAH-RDPLAMQQFFAEYGVTTT---HFVPSMLAAF 700
Cdd:cd05906 198 GKIQHNGLTPQDVFLNWVPLDHVGGLVELhLRAVYLGCQQVHVPTEEIlADPLRWLDLIDRYRVTITwapNFAFALLNDL 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 701 VASLTPQTARQSCatLKQVFCSGEALPADLCREWQQL---TGAP---LHNLYGPTEAAVDVSWYPAFGEELAQVRGSSVP 774
Cdd:cd05906 278 LEEIEDGTWDLSS--LRYLVNAGEAVVAKTIRRLLRLlepYGLPpdaIRPAFGMTETCSGVIYSRSFPTYDHSQALEFVS 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 775 IGYPVWNTGLRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermYRTGDVArWLDNGAVEYLG 854
Cdd:cd05906 356 LGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGW------FRTGDLG-FLDNGNLTITG 428
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128569 855 RSDDQLKIRGQRIELGEIDRVMQALPDVEQAVTHACVINQAaatGGDARQLVGYLVSQSGLPLDTSALQAQLRETL 930
Cdd:cd05906 429 RTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSFTAAFAVRDP---GAETEELAIFFVPEYDLQDALSETLRAIRSVV 501
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
461-930 |
3.03e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 123.38 E-value: 3.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 461 VAEQAAKTPDAPA---LADARYlFSYREMREQVVALANLLRERGVKPGDSVAVaLPRSVFLTLALH-AIVEAGAAWLPLD 536
Cdd:PRK09088 1 IAFHARLQPQRLAavdLALGRR-WTYAELDALVGRLAAVLRRRGCVDGERLAV-LARNSVWLVALHfACARVGAIYVPLN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 537 TGYPDDRLKMMLEDARPSLLITTDDQLPRFSDVPNLTSLCYNA-PLTPQGSAPLQlsqPHHTAYIIFTSGSTGRPKGVMV 615
Cdd:PRK09088 79 WRLSASELDALLQDAEPRLLLGDDAVAAGRTDVEDLAAFIASAdALEPADTPSIP---PERVSLILFTSGTSGQPKGVML 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 616 G-----QTAIVNRLLWMQNHypltgEDVVAQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAhrDPLAMQQFFAEYGVTTT 690
Cdd:PRK09088 156 SernlqQTAHNFGVLGRVDA-----HSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGF--EPKRTLGRLGDPALGIT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 691 HF--VPSMLAAFVASltPQTARQSCATLKQVFCSGEALPADLCREWQQlTGAPLHNLYGPTEAAVdVSWYPAFGEELAQV 768
Cdd:PRK09088 229 HYfcVPQMAQAFRAQ--PGFDAAALRHLTALFTGGAPHAAEDILGWLD-DGIPMVDGFGMSEAGT-VFGMSVDCDVIRAK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 769 RGSSvpiGYPVWNTGLRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermYRTGDVARWLDNG 848
Cdd:PRK09088 305 AGAA---GIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGW------FRTGDIARRDADG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 849 AVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQAVthacVINQAAATGGDarqlVGYL--VSQSGLPLDTSALQAQL 926
Cdd:PRK09088 376 FFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECA----VVGMADAQWGE----VGYLaiVPADGAPLDLERIRSHL 447
|
....
gi 16128569 927 RETL 930
Cdd:PRK09088 448 STRL 451
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
438-928 |
4.21e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 124.00 E-value: 4.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 438 EYAQLAQLNATQ-----------VEIP--ETTLSALVAEQAAKTPDAPALADARYLFSYREMREQVVALANLLRERGVKP 504
Cdd:PRK06178 3 EEAYLAELRALQqaawpagiprePEYPhgERPLTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 505 GDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTDDQLPRFSDVPNLTSL--------- 575
Cdd:PRK06178 83 GDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRAETSLrhvivtsla 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 576 ---------------------------CYNAPLTPQGSAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRllwMQ 628
Cdd:PRK06178 163 dvlpaeptlplpdslraprlaaagaidLLPALRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYT---AA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 629 NHYPLT---GEDVVAqktpcsfdVSVWEFFW----------PFIAGAKLVMAepeAHRDPLAMQQFFAEYGVTTThfvpS 695
Cdd:PRK06178 240 AAYAVAvvgGEDSVF--------LSFLPEFWiagenfgllfPLFSGATLVLL---ARWDAVAFMAAVERYRVTRT----V 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 696 MLAAFVASL--TPQTARQSCATLKQVFCSG--EALPADLCREWQQLTGAPLHNL-YGPTEAAVDVSWYPAFGEELAQVRG 770
Cdd:PRK06178 305 MLVDNAVELmdHPRFAEYDLSSLRQVRVVSfvKKLNPDYRQRWRALTGSVLAEAaWGMTETHTCDTFTAGFQDDDFDLLS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 771 SSVPIGYPVWNTGLRILDAMMH-PVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIadpfapgERMYRTGDVARWLDNGA 849
Cdd:PRK06178 385 QPVFVGLPVPGTEFKICDFETGeLLPLGAEGEIVVRTPSLLKGYWNKPEATAEALR-------DGWLHTGDIGKIDEQGF 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128569 850 VEYLGRSDDQLKIRGQRIELGEIDRVMQALPdveqAVTHACVINQAAATGGdaRQLVGYLVSQSGLPLDTSALQAQLRE 928
Cdd:PRK06178 458 LHYLGRRKEMLKVNGMSVFPSEVEALLGQHP----AVLGSAVVGRPDPDKG--QVPVAFVQLKPGADLTAAALQAWCRE 530
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
452-892 |
8.03e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 123.15 E-value: 8.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 452 IPETTLSALVAEQAAKTPDAPALA--DARYlfSYREMREQVVALANLL-RERGVKPGDSVAVALPRSVFLTLALHAIVEA 528
Cdd:PRK08314 7 LPETSLFHNLEVSARRYPDKTAIVfyGRAI--SYRELLEEAERLAGYLqQECGVRKGDRVLLYMQNSPQFVIAYYAILRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 529 GAAWLPLDTGYPDDRLKMMLEDARPSLLITTDDQLPRFSDVPNLTSL------CYNAPLTPQGS----------APLQ-- 590
Cdd:PRK08314 85 NAVVVPVNPMNREEELAHYVTDSGARVAIVGSELAPKVAPAVGNLRLrhvivaQYSDYLPAEPEiavpawlraePPLQal 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 591 ---------------LSQPHHT------AYIIFTSGSTGRPKGVM----VGQTAIVNRLLWMQnhypLTGEDVVaqktpc 645
Cdd:PRK08314 165 apggvvawkealaagLAPPPHTagpddlAVLPYTSGTTGVPKGCMhthrTVMANAVGSVLWSN----STPESVV------ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 646 sfdVSVWEFFW----------PFIAGAKLVMAePEAHRDPLAmqQFFAEYGVTTTHFVPSMLAAFVASltPQTARQSCAT 715
Cdd:PRK08314 235 ---LAVLPLFHvtgmvhsmnaPIYAGATVVLM-PRWDREAAA--RLIERYRVTHWTNIPTMVVDFLAS--PGLAERDLSS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 716 LKQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVDVSWYPAfgeelaqVRGSSVPIGYPVWNTGLRILD-AMMHPV 794
Cdd:PRK08314 307 LRYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTETMAQTHSNPP-------DRPKLQCLGIPTFGVDARVIDpETLEEL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 795 PPGVAGDLYLTGIQLAQGYLGRPDLTASRFIAdpfAPGERMYRTGDvarwldngaveyLGRSD--------DQLK----I 862
Cdd:PRK08314 380 PPGEVGEIVVHGPQVFKGYWNRPEATAEAFIE---IDGKRFFRTGD------------LGRMDeegyffitDRLKrminA 444
|
490 500 510
....*....|....*....|....*....|
gi 16128569 863 RGQRIELGEIDRVMQALPDVEQavthACVI 892
Cdd:PRK08314 445 SGFKVWPAEVENLLYKHPAIQE----ACVI 470
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
454-885 |
3.04e-28 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 121.02 E-value: 3.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 454 ETTLSALVAEQAAKTPDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALP-RSVFLTLALhaiveaGAAW 532
Cdd:PRK06155 20 ERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGnRIEFLDVFL------GCAW 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 533 L-----PLDTGYPDDRLKMMLEDARPSLLITTDDQLPRF-----------------SDVPNLTSLCYNAPLTPQGSAPLQ 590
Cdd:PRK06155 94 LgaiavPINTALRGPQLEHILRNSGARLLVVEAALLAALeaadpgdlplpavwlldAPASVSVPAGWSTAPLPPLDAPAP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 591 LS--QPHHTAYIIFTSGSTGRPKGVMVGQTaivnRLLW----MQNHYPLTGEDVVAQKTPCSFDVSVWEFFWPFIAGAKL 664
Cdd:PRK06155 174 AAavQPGDTAAILYTSGTTGPSKGVCCPHA----QFYWwgrnSAEDLEIGADDVLYTTLPLFHTNALNAFFQALLAGATY 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 665 VMAEpeahrdPLAMQQFFA---EYGVTTTHFVPSMLAAFVASltPQTARQSCATLKQVFcsGEALPADLCREWQQLTGAP 741
Cdd:PRK06155 250 VLEP------RFSASGFWPavrRHGATVTYLLGAMVSILLSQ--PARESDRAHRVRVAL--GPGVPAALHAAFRERFGVD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 742 LHNLYGPTEAAVdvswypAFGEELAQVRGSSvpIGYPVWNTGLRILDAMMHPVPPGVAGDLYLTGIQ---LAQGYLGRPD 818
Cdd:PRK06155 320 LLDGYGSTETNF------VIAVTHGSQRPGS--MGRLAPGFEARVVDEHDQELPDGEPGELLLRADEpfaFATGYFGMPE 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128569 819 LTASRFIADPFAPGERMYRTGDvarwldnGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQA 885
Cdd:PRK06155 392 KTVEAWRNLWFHTGDRVVRDAD-------GWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAA 451
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
482-887 |
3.71e-28 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 120.13 E-value: 3.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 482 SYREMREQVVALANLLrERGVKPGDSVAVALPRS-----VFLTLAL--------------------------------HA 524
Cdd:cd05909 9 TYRKLLTGAIALARKL-AKMTKEGENVGVMLPPSaggalANFALALsgkvpvmlnytaglrelraciklagiktvltsKQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 525 IVEAGAAWLPLDTGYPddrLKMM-LEDARPSllITTDDQLprfsdvpnLTSLCYNAPLTP----QGSAPLQLSQPhhtAY 599
Cdd:cd05909 88 FIEKLKLHHLFDVEYD---ARIVyLEDLRAK--ISKADKC--------KAFLAGKFPPKWllriFGVAPVQPDDP---AV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 600 IIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTGEDVVAQKTPC----SFDVSVWeffWPFIAGAKLVMaepeaHRDP 675
Cdd:cd05909 152 ILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFfhsfGLTGCLW---LPLLSGIKVVF-----HPNP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 676 LAMQQ---FFAEYGVTTTHFVPSMLAAFVASLTPQTArqscATLKQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEA- 751
Cdd:cd05909 224 LDYKKipeLIYDKKATILLGTPTFLRGYARAAHPEDF----SSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECs 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 752 ---AVDVSWYPAfgeelaqvRGSSVpiGYPVWNTGLRILDAMMH-PVPPGVAGDLYLTGIQLAQGYLGRPDLTAsrfiad 827
Cdd:cd05909 300 pviSVNTPQSPN--------KEGTV--GRPLPGMEVKIVSVETHeEVPIGEGGLLLVRGPNVMLGYLNEPELTS------ 363
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128569 828 pFAPGERMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEI-DRVMQALP-DVEQAVT 887
Cdd:cd05909 364 -FAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIeDILSEILPeDNEVAVV 424
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
454-890 |
7.95e-28 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 119.85 E-value: 7.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 454 ETTLSALVAEQAAKTPDAPALADAR-YLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAW 532
Cdd:PRK06087 22 DASLADYWQQTARAMPDKIAVVDNHgASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 533 LPLDTGYPDDRLK--MMLEDAR----PSLLITTDDQ---LPRFSDVPNLTSLCY---NAPLTP--------QGSAPLQLS 592
Cdd:PRK06087 102 VPLLPSWREAELVwvLNKCQAKmffaPTLFKQTRPVdliLPLQNQLPQLQQIVGvdkLAPATSslslsqiiADYEPLTTA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 593 QPHHT---AYIIFTSGSTGRPKGVMVGQtaivNRLLWMQNHY----PLTGEDVVAQKTPCSFDVSvweFFW----PFIAG 661
Cdd:PRK06087 182 ITTHGdelAAVLFTSGTEGLPKGVMLTH----NNILASERAYcarlNLTWQDVFMMPAPLGHATG---FLHgvtaPFLIG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 662 AKLVMAEpeaHRDPLAMQQFFAEYGVT----TTHFVPSMLAAfvasLTPQTARQScaTLKQVFCSGEALPADLCREWQQl 737
Cdd:PRK06087 255 ARSVLLD---IFTPDACLALLEQQRCTcmlgATPFIYDLLNL----LEKQPADLS--ALRFFLCGGTTIPKKVARECQQ- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 738 TGAPLHNLYGPTEAAVDVswYPAFGEELAQVRGSSvpiGYPVWNTGLRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRP 817
Cdd:PRK06087 325 RGIKLLSVYGSTESSPHA--VVNLDDPLSRFMHTD---GYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEP 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128569 818 DLTASRFIADPFapgermYRTGDVARWLDNGAVEYLGRSDDqLKIR-GQRIELGEIDRVMQALPDVEQAVTHAC 890
Cdd:PRK06087 400 ELTARALDEEGW------YYSGDLCRMDEAGYIKITGRKKD-IIVRgGENISSREVEDILLQHPKIHDACVVAM 466
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
481-892 |
9.94e-28 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 117.99 E-value: 9.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 481 FSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTD 560
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 561 DQLPRFSdvpnltslcynapltpqgsaplqlsqPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTGEDVVA 640
Cdd:cd05969 81 ELYERTD--------------------------PEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIYW 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 641 qktpCSFDV-----SVWEFFWPFIAGAKLVMAEPEAhrDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPQTARQSCAT 715
Cdd:cd05969 135 ----CTADPgwvtgTVYGIWAPWLNGVTNVVYEGRF--DAESWYGIIERVKVTVWYTAPTAIRMLMKEGDELARKYDLSS 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 716 LKQVFCSGEALPADLCREWQQLTGAPLHNLYGPTE-AAVDVSWYPAFgeelaQVRGSSvpIGYPVWNTGLRILDAMMHPV 794
Cdd:cd05969 209 LRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTEtGSIMIANYPCM-----PIKPGS--MGKPLPGVKAAVVDENGNEL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 795 PPGVAGDLYLTG--IQLAQGYLGRPDLTASRFIadpfapgERMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEI 872
Cdd:cd05969 282 PPGTKGILALKPgwPSMFRGIWNDEERYKNSFI-------DGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEV 354
|
410 420
....*....|....*....|
gi 16128569 873 DRVMQALPdveqAVTHACVI 892
Cdd:cd05969 355 ESALMEHP----AVAEAGVI 370
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
452-958 |
1.37e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 118.94 E-value: 1.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 452 IPETTLSALvaeqaAKTPDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAA 531
Cdd:PRK06188 14 YGHLLVSAL-----KRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 532 WLPLDT-GYPDDRLkMMLEDARPSLLITTDDQ--------LPRFSDVPNLTSLC-------YNAPLTPQGSAPLQ-LSQP 594
Cdd:PRK06188 89 RTALHPlGSLDDHA-YVLEDAGISTLIVDPAPfveralalLARVPSLKHVLTLGpvpdgvdLLAAAAKFGPAPLVaAALP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 595 HHTAYIIFTSGSTGRPKGVMvgqtaIVNRLLWMQNHYPLTgedvvaqktpcsfdvsvwEFFWPfiAGAKLVMAEPEAHR- 673
Cdd:PRK06188 168 PDIAGLAYTGGTTGKPKGVM-----GTHRSIATMAQIQLA------------------EWEWP--ADPRFLMCTPLSHAg 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 674 --------------------DPLAMQQFFAEYGVTTTHFVPSMLAAFVASltPQTARQSCATLKQVFCSGEALPADLCRE 733
Cdd:PRK06188 223 gafflptllrggtvivlakfDPAEVLRAIEEQRITATFLVPTMIYALLDH--PDLRTRDLSSLETVYYGASPMSPVRLAE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 734 WQQLTGAPLHNLYGPTEAAVDVSWYPAFGEELAQVR--GSSvpiGYPVWNTGLRILDAMMHPVPPGVAGDLYLTGIQLAQ 811
Cdd:PRK06188 301 AIERFGPIFAQYYGQTEAPMVITYLRKRDHDPDDPKrlTSC---GRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMD 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 812 GYLGRPDLTasrfiADPFAPGerMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQavthACV 891
Cdd:PRK06188 378 GYWNRPEET-----AEAFRDG--WLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQ----VAV 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128569 892 INQAAATGGDArqLVGYLVSQSGLPLDTSALQAQLRETLPPHMVPVVLLQLPQLPLSANGKLDRKAL 958
Cdd:PRK06188 447 IGVPDEKWGEA--VTAVVVLRPGAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKAL 511
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
461-885 |
1.69e-27 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 118.42 E-value: 1.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 461 VAEQAAKTPDAPALADARYLFSYREMREQVVALANLLRER-GVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGY 539
Cdd:PRK06839 8 IEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 540 PDDRLKMMLED------------ARPSLLITTDDQLPRFSDVPNLTSLCYNAPLT---PQGSAPLqlsqphhtaYIIFTS 604
Cdd:PRK06839 88 TENELIFQLKDsgttvlfvektfQNMALSMQKVSYVQRVISITSLKEIEDRKIDNfveKNESASF---------IICYTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 605 GSTGRPKGVMVGQTAI----VNRLLWMQnhypLTGEDVVAQKTPCSFDVSVWEFFWP-FIAGAKLVMAEpeaHRDPLAMQ 679
Cdd:PRK06839 159 GTTGKPKGAVLTQENMfwnaLNNTFAID----LTMHDRSIVLLPLFHIGGIGLFAFPtLFAGGVIIVPR---KFEPTKAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 680 QFFAEYGVTTTHFVPSMLAAFVASltPQTARQSCATLKQVFCSGEALPADLCREWQQlTGAPLHNLYGPTEAAVDVswYP 759
Cdd:PRK06839 232 SMIEKHKVTVVMGVPTIHQALINC--SKFETTNLQSVRWFYNGGAPCPEELMREFID-RGFLFGQGFGMTETSPTV--FM 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 760 AFGEELAQVRGSsvpIGYPVWNTGLRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRfIADPFapgermYRTG 839
Cdd:PRK06839 307 LSEEDARRKVGS---IGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEET-IQDGW------LCTG 376
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 16128569 840 DVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQA 885
Cdd:PRK06839 377 DLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEV 422
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
456-898 |
2.99e-27 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 117.72 E-value: 2.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 456 TLSALVAEQAAKTPDAPALADAR--YLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWL 533
Cdd:cd05904 6 PLDSVSFLFASAHPSRPALIDAAtgRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 534 PLDTGYPDDRLKMMLEDARPSLLITTDDQLPRFSDVPNLTSLCYNAP-----------LTPQGSAPLQLSQPHHTAYIIF 602
Cdd:cd05904 86 TANPLSTPAEIAKQVKDSGAKLAFTTAELAEKLASLALPVVLLDSAEfdslsfsdllfEADEAEPPVVVIKQDDVAALLY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 603 TSGSTGRPKGVM------VGQTAIVNRLLWMQNHYpltgEDVVAqktpcsfdvsvweFFWPFI--------------AGA 662
Cdd:cd05904 166 SSGTTGRSKGVMlthrnlIAMVAQFVAGEGSNSDS----EDVFL-------------CVLPMFhiyglssfalgllrLGA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 663 KLVmaepeahrdplAMQQFFAE--------YGVTTTHFVPSMLAAFVASltPQTARQSCATLKQVFCSGEALPADLCREW 734
Cdd:cd05904 229 TVV-----------VMPRFDLEellaaierYKVTHLPVVPPIVLALVKS--PIVDKYDLSSLRQIMSGAAPLGKELIEAF 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 735 -QQLTGAPLHNLYGPTEA-AVDVSwypAFGEELAQVRGSSVpiGYPVWNTGLRILD-AMMHPVPPGVAGDLYLTGIQLAQ 811
Cdd:cd05904 296 rAKFPNVDLGQGYGMTEStGVVAM---CFAPEKDRAKYGSV--GRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMK 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 812 GYLGRPDLTASRFIADPFapgermYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQA------ 885
Cdd:cd05904 371 GYLNNPEATAATIDKEGW------LHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAavipyp 444
|
490
....*....|....*....
gi 16128569 886 ------VTHACVINQAAAT 898
Cdd:cd05904 445 deeageVPMAFVVRKPGSS 463
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
481-891 |
1.36e-26 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 115.81 E-value: 1.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 481 FSYREMREQVVALANLLRERGVKPGDSVAV-------------ALP---------------------------RSVFLTL 520
Cdd:cd12119 26 YTYAEVAERARRLANALRRLGVKPGDRVATlawnthrhlelyyAVPgmgavlhtinprlfpeqiayiinhaedRVVFVDR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 521 ALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTDDQLPRFSDVpnltslcYNAPLTPQGSAplqlsqphhtAYI 600
Cdd:cd12119 106 DFLPLLEAIAPRLPTVEHVVVMTDDAAMPEPAGVGVLAYEELLAAESPE-------YDWPDFDENTA----------AAI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 601 IFTSGSTGRPKGVMVGQTAIVnrL----LWMQNHYPLTGEDVVAQKTPCsFDVSVWEFfwPFIA---GAKLVMaePEAHR 673
Cdd:cd12119 169 CYTSGTTGNPKGVVYSHRSLV--LhamaALLTDGLGLSESDVVLPVVPM-FHVNAWGL--PYAAamvGAKLVL--PGPYL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 674 DPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPQTARQScaTLKQVFCSGEALPADLCREWQQLtGAPLHNLYGPTEAA- 752
Cdd:cd12119 242 DPASLAELIEREGVTFAAGVPTVWQGLLDHLEANGRDLS--SLRRVVIGGSAVPRSLIEAFEER-GVRVIHAWGMTETSp 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 753 -VDVSWYPAF-----GEELAQVRGSSvpiGYPVWNTGLRILDAMMHPVP--PGVAGDLYLTGIQLAQGYLGRPDlTASRF 824
Cdd:cd12119 319 lGTVARPPSEhsnlsEDEQLALRAKQ---GRPVPGVELRIVDDDGRELPwdGKAVGELQVRGPWVTKSYYKNDE-ESEAL 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128569 825 IADPFapgermYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQAvthACV 891
Cdd:cd12119 395 TEDGW------LRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEA---AVI 452
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
7-200 |
1.55e-26 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 109.74 E-value: 1.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 7 LVAAQPGIWMAEKLSelpSAWSVAHYVELTGEVDSPLLARAVVAGLAQADTLRMRFTEDNGEVWQWVDDALTFELpEIID 86
Cdd:COG4908 1 LSPAQKRFLFLEPGS---NAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADLPL-EVVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 87 LR--TNIDPHGTAQALMQADLQQDLRVDSGkPLVFHQLIQVADNRWYWYQRYHHLLVDGFSFPAITRQIANIYCTWLRGE 164
Cdd:COG4908 77 LSalPEPEREAELEELVAEEASRPFDLARG-PLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGE 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 16128569 165 PTPASPFT-PFADVVEEYQQYRESEAWQRDAAFWAEQ 200
Cdd:COG4908 156 PPPLPELPiQYADYAAWQRAWLQSEALEKQLEYWRQQ 192
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
481-892 |
3.10e-26 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 113.38 E-value: 3.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 481 FSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTD 560
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 561 DQLPRFSDVPNLtslcynapltpqgsaplqlsqphhtayIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTGEDVVA 640
Cdd:cd05973 81 ANRHKLDSDPFV---------------------------MMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSFW 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 641 qktpCSFDVSvWEFFWPFIAGAKLVMAEP----EAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPQTARQScATL 716
Cdd:cd05973 134 ----NAADPG-WAYGLYYAITGPLALGHPtillEGGFSVESTWRVIERLGVTNLAGSPTAYRLLMAAGAEVPARPK-GRL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 717 KQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVDVSWYPAFGEELAQvrGSSvpiGYPVWNTGLRILDAMMHPVPP 796
Cdd:cd05973 208 RRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVLANHHALEHPVHA--GSA---GRAMPGWRVAVLDDDGDELGP 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 797 GVAG----DLYLTGIQLAQGYLGRPDLTASrfiadpfapgERMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEI 872
Cdd:cd05973 283 GEPGrlaiDIANSPLMWFRGYQLPDTPAID----------GGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDV 352
|
410 420
....*....|....*....|
gi 16128569 873 DRVMQALPdveqAVTHACVI 892
Cdd:cd05973 353 ESALIEHP----AVAEAAVI 368
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
454-932 |
4.12e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 111.37 E-value: 4.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 454 ETTLSALVAEQAAKTPDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALP-RSVFLTLAL---------- 522
Cdd:PRK06164 9 ADTLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPnCIEWVVLFLacarlgatvi 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 523 ------------HAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLIT---------TDDQLPRFSDVPNLTSLCYNAPL 581
Cdd:PRK06164 89 avntryrshevaHILGRGRARWLVVWPGFKGIDFAAILAAVPPDALPPlraiavvddAADATPAPAPGARVQLFALPDPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 582 TPQGSAPLQlSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTGEDVVAQKTPCSFDVSVWEFFWPFIAG 661
Cdd:PRK06164 169 PPAAAGERA-ADPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 662 AKLVMaepEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAfVASLTPQtaRQSCATLKqVFCSGEALPA--DLCrEWQQLTG 739
Cdd:PRK06164 248 APLVC---EPVFDAARTARALRRHRVTHTFGNDEMLRR-ILDTAGE--RADFPSAR-LFGFASFAPAlgELA-ALARARG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 740 APLHNLYGPTEAAVDVSWYPAFGEELAQVRGSSVPIgYPvwNTGLRILDAMMHPV-PPGVAGDLYLTGIQLAQGYLGRPD 818
Cdd:PRK06164 320 VPLTGLYGSSEVQALVALQPATDPVSVRIEGGGRPA-SP--EARVRARDPQDGALlPDGESGEIEIRAPSLMRGYLDNPD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 819 LTASRFIADPFapgermYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVeqavtHACVInQAAAT 898
Cdd:PRK06164 397 ATARALTDDGY------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGV-----AAAQV-VGATR 464
|
490 500 510
....*....|....*....|....*....|....
gi 16128569 899 GGDARQlVGYLVSQSGLPLDTSALQAQLRETLPP 932
Cdd:PRK06164 465 DGKTVP-VAFVIPTDGASPDEAGLMAACREALAG 497
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
471-958 |
6.03e-25 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 109.49 E-value: 6.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 471 APALADARYLFSYREMREQVVALAN-LLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGA---AWLPL----DTGYPdd 542
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIANvLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAiavATMPLlrpkELAYI-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 543 rlkmmLEDARPSLLITtDDQLPRFSDVpnltslcynapltpqgsaplqlsqphhtAYIIFTSGSTGRPKGVM-VGQTAIV 621
Cdd:cd05958 79 -----LDKARITVALC-AHALTASDDI----------------------------CILAFTSGTTGAPKATMhFHRDPLA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 622 NRLLWMQNHYPLTGEDVVAQKTPCSFDVSV-WEFFWPFIAGAKLVMAEpeaHRDPLAMQQFFAEYGVTTTHFVPSMLAAF 700
Cdd:cd05958 125 SADRYAVNVLRLREDDRFVGSPPLAFTFGLgGVLLFPFGVGASGVLLE---EATPDLLLSAIARYKPTVLFTAPTAYRAM 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 701 VASltPQTARQSCATLKQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAavdVSWYPAFGEELAQVrGSSvpiGYPVW 780
Cdd:cd05958 202 LAH--PDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEM---FHIFISARPGDARP-GAT---GKPVP 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 781 NTGLRILDAMMHPVPPGVAGDLYLTGiqlaqgylgrPdlTASRFIADP----FAPGERMYrTGDVARWLDNGAVEYLGRS 856
Cdd:cd05958 273 GYEAKVVDDEGNPVPDGTIGRLAVRG----------P--TGCRYLADKrqrtYVQGGWNI-TGDTYSRDPDGYFRHQGRS 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 857 DDQLKIRGQRIELGEIDRVMQALPDVEQAVTHACVInqaaatggDARQLV--GYLVSQSGL---PLDTSALQAQLRETLP 931
Cdd:cd05958 340 DDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPD--------ESRGVVvkAFVVLRPGVipgPVLARELQDHAKAHIA 411
|
490 500
....*....|....*....|....*..
gi 16128569 932 PHMVPVVLLQLPQLPLSANGKLDRKAL 958
Cdd:cd05958 412 PYKYPRAIEFVTELPRTATGKLQRFAL 438
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
456-912 |
6.13e-25 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 111.01 E-value: 6.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 456 TLSALVAEQAAKTPDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAawLPL 535
Cdd:COG1021 26 TLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGA--IPV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 536 DTgYPDDR---LKMMLEDARPSLLITtDDQLPRF----------SDVPNL------------TSL--CYNAPLTPQGSAP 588
Cdd:COG1021 104 FA-LPAHRraeISHFAEQSEAVAYII-PDRHRGFdyralarelqAEVPSLrhvlvvgdagefTSLdaLLAAPADLSEPRP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 589 -------LQLSqphhtayiiftSGSTGRPKGV---------MVGQTAIVNRLlwmqnhyplTGEDV--VAQKTPCSFDVS 650
Cdd:COG1021 182 dpddvafFQLS-----------GGTTGLPKLIprthddylySVRASAEICGL---------DADTVylAALPAAHNFPLS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 651 VWEFFWPFIAGAKLVMAEpeahrDPLAMQQF--FAEYGVTTTHFVPSMLAAFVASltPQTARQSCATLKQVFCSGEALPA 728
Cdd:COG1021 242 SPGVLGVLYAGGTVVLAP-----DPSPDTAFplIERERVTVTALVPPLALLWLDA--AERSRYDLSSLRVLQVGGAKLSP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 729 DLCREWQQLTGAPLHNLYGPTEAAVDvswYPAFGEELAQVRGSsvpIGYPV--WNTgLRILDAMMHPVPPGVAGDLYLTG 806
Cdd:COG1021 315 ELARRVRPALGCTLQQVFGMAEGLVN---YTRLDDPEEVILTT---QGRPIspDDE-VRIVDEDGNPVPPGEVGELLTRG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 807 IQLAQGYLGRPDLTASRFIADPFapgermYRTGDVARWLDNGAVEYLGRSDDQLkIR-GQRIELGEIDRVMQALPDVEQA 885
Cdd:COG1021 388 PYTIRGYYRAPEHNARAFTPDGF------YRTGDLVRRTPDGYLVVEGRAKDQI-NRgGEKIAAEEVENLLLAHPAVHDA 460
|
490 500 510
....*....|....*....|....*....|....*....
gi 16128569 886 V------------THACVINQAAATggDARQLVGYLVSQ 912
Cdd:COG1021 461 AvvampdeylgerSCAFVVPRGEPL--TLAELRRFLRER 497
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
465-930 |
7.38e-25 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 110.79 E-value: 7.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 465 AAKTPDAPALadaRYL---------FSYREMREQVVALANLLRERGvKPGDSVAVALPRSVFLTLALHAIVEAG--AAWL 533
Cdd:cd05931 3 AAARPDRPAY---TFLddeggreetLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGaiAVPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 534 PLDTGYP-DDRLKMMLEDARPSLLITTDDQLPRF--------SDVPNLTSLCYNAPLTPQGSAPLQLSQPHHTAYIIFTS 604
Cdd:cd05931 79 PPPTPGRhAERLAAILADAGPRVVLTTAAALAAVrafaasrpAAGTPRLLVVDLLPDTSAADWPPPSPDPDDIAYLQYTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 605 GSTGRPKGVMVGQTAIVNRLLWMQNHYPLTGEDVVAQKTPCSFDVSVWEF-FWPFIAGAKLVMAEPEAH-RDPLAMQQFF 682
Cdd:cd05931 159 GSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGlLTPLYSGGPSVLMSPAAFlRRPLRWLRLI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 683 AEYGVTTThFVPSMlaAF---VASLTP-QTARQSCATLKQVFCSGEALPADLCREWQQlTGAPlHNL--------YGPTE 750
Cdd:cd05931 239 SRYRATIS-AAPNF--AYdlcVRRVRDeDLEGLDLSSWRVALNGAEPVRPATLRRFAE-AFAP-FGFrpeafrpsYGLAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 751 AAVDVSWYPA--------FGEELAQVRGSSVPI-----------GYPVWNTGLRILDAMMH-PVPPGVAGDLYLTGIQLA 810
Cdd:cd05931 314 ATLFVSGGPPgtgpvvlrVDRDALAGRAVAVAAddpaarelvscGRPLPDQEVRIVDPETGrELPDGEVGEIWVRGPSVA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 811 QGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDnGAVEYLGRSDDQLKIRGQRIelgeidrvmqaLP-DVEQAVTHA 889
Cdd:cd05931 394 SGYWGRPEATAETFGALAATDEGGWLRTGDLGFLHD-GELYITGRLKDLIIVRGRNH-----------YPqDIEATAEEA 461
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 16128569 890 C---VINQAAA---TGGDARQLV-GYLVSQSGLPLDTSALQAQLRETL 930
Cdd:cd05931 462 HpalRPGCVAAfsvPDDGEERLVvVAEVERGADPADLAAIAAAIRAAV 509
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
481-886 |
7.63e-25 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 110.54 E-value: 7.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 481 FSYREMREQVVALANLLRERGVKPGDSVAVAL---PRSVFLTLALHAIveaGAAWLPLDTGYPDDRLKMMLEDARPSLLI 557
Cdd:PRK08008 38 YSYLELNEEINRTANLFYSLGIRKGDKVALHLdncPEFIFCWFGLAKI---GAIMVPINARLLREESAWILQNSQASLLV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 558 T------------------------TDDQLPRFSDVPNLTSLCYNAPLTPQGSAPLQlsqPHHTAYIIFTSGSTGRPKGV 613
Cdd:PRK08008 115 TsaqfypmyrqiqqedatplrhiclTRVALPADDGVSSFTQLKAQQPATLCYAPPLS---TDDTAEILFTSGTTSRPKGV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 614 MvgqtaIVNRLLWMQNHYP-----LTGEDVVAQKTP-CSFDVSVWEFFWPFIAGAKLVMAEPEAHRdplAMQQFFAEYGV 687
Cdd:PRK08008 192 V-----ITHYNLRFAGYYSawqcaLRDDDVYLTVMPaFHIDCQCTAAMAAFSAGATFVLLEKYSAR---AFWGQVCKYRA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 688 TTTHFVPSMLAAFVasLTPQTA--RQSCatLKQVFCS---GEALPADLCREWqqltGAPLHNLYGPTEAAVDVSWYPAFG 762
Cdd:PRK08008 264 TITECIPMMIRTLM--VQPPSAndRQHC--LREVMFYlnlSDQEKDAFEERF----GVRLLTSYGMTETIVGIIGDRPGD 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 763 EElaqvRGSSvpIGYPVWNTGLRILDAMMHPVPPGVAGDLYLTGI---QLAQGYLGRPDLTASRFIADPFapgermYRTG 839
Cdd:PRK08008 336 KR----RWPS--IGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVpgkTIFKEYYLDPKATAKVLEADGW------LHTG 403
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 16128569 840 DVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQAV 886
Cdd:PRK08008 404 DTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIV 450
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
456-930 |
9.51e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 109.98 E-value: 9.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 456 TLSALVAEQAAKTPDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSV-FLTLALhAIVEAGAAWLP 534
Cdd:PRK06145 3 NLSASIAFHARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAaFLELAF-AASYLGAVFLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 535 LDTGYPDDRLKMMLEDARPSLLITTDDqlprFSDVPNLTSLCYNAPLTPQGS-----------APLQLSQPHHTAYIIFT 603
Cdd:PRK06145 82 INYRLAADEVAYILGDAGAKLLLVDEE----FDAIVALETPKIVIDAAAQADsrrlaqggleiPPQAAVAPTDLVRLMYT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 604 SGSTGRPKGVMVGqtaiVNRLLWMQNHYP----LTGEDVVAQKTPC----SFDVSVWEFFWpfIAGAKLVMAEpeahRDP 675
Cdd:PRK06145 158 SGTTDRPKGVMHS----YGNLHWKSIDHVialgLTASERLLVVGPLyhvgAFDLPGIAVLW--VGGTLRIHRE----FDP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 676 LAMQQFFAEYGVTTTHFVPSMLAAFVAslTPQTARQSCATLKQVFCSGEALPADLCREWQQL-TGAPLHNLYGPTEAAVD 754
Cdd:PRK06145 228 EAVLAAIERHRLTCAWMAPVMLSRVLT--VPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVfTRARYIDAYGLTETCSG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 755 VSWYPAfGEELAQVrGSSvpiGYPVWNTGLRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFapger 834
Cdd:PRK06145 306 DTLMEA-GREIEKI-GST---GRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF----- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 835 myRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQAVthacVINQAAATGGDarQLVGYLVSQSG 914
Cdd:PRK06145 376 --RSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAA----VIGVHDDRWGE--RITAVVVLNPG 447
|
490
....*....|....*.
gi 16128569 915 LPLDTSALQAQLRETL 930
Cdd:PRK06145 448 ATLTLEALDRHCRQRL 463
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
462-886 |
1.30e-24 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 110.48 E-value: 1.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 462 AEQAAKTPDAPaLADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPD 541
Cdd:cd05967 65 GDQIALIYDSP-VTGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 542 DRLKMMLEDARPSLLITTD---------------DQLPRFSDVPNLTSLCYNAPLTPQG----------SAPLQLSQPH- 595
Cdd:cd05967 144 KELASRIDDAKPKLIVTAScgiepgkvvpykpllDKALELSGHKPHHVLVLNRPQVPADltkpgrdldwSELLAKAEPVd 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 596 -------HTAYIIFTSGSTGRPKGVM--VGQTAIVnrLLW-MQNHYPLTGEDVVAqktpCSFDVSvweffW--------- 656
Cdd:cd05967 224 cvpvaatDPLYILYTSGTTGKPKGVVrdNGGHAVA--LNWsMRNIYGIKPGDVWW----AASDVG-----Wvvghsyivy 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 657 -PFIAGAKLVMAE--PEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAF-VASLTPQTARQ-SCATLKQVFCSGEALPADlC 731
Cdd:cd05967 293 gPLLHGATTVLYEgkPVGTPDPGAFWRVIEKYQVNALFTAPTAIRAIrKEDPDGKYIKKyDLSSLRTLFLAGERLDPP-T 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 732 REW-QQLTGAPLHNLYGPTEAAVDVSWYPAFGEELAQVRGSS-VPI-GYPVwntglRILDAMMHPVPPGVAGDLYLTGiQ 808
Cdd:cd05967 372 LEWaENTLGVPVIDHWWQTETGWPITANPVGLEPLPIKAGSPgKPVpGYQV-----QVLDEDGEPVGPNELGNIVIKL-P 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 809 LAQGYLGRPDLTASRFIADPFA--PGerMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDV-EQA 885
Cdd:cd05967 446 LPPGCLLTLWKNDERFKKLYLSkfPG--YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVaECA 523
|
.
gi 16128569 886 V 886
Cdd:cd05967 524 V 524
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
447-930 |
1.42e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 110.09 E-value: 1.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 447 ATQVEIPETTLSALVAEQAAKTPDAPALadarYLF----SYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLAL 522
Cdd:PRK05605 24 PHDLDYGDTTLVDLYDNAVARFGDRPAL----DFFgattTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 523 HAIVEAGAAWL---PLdtgYPDDRLKMMLEDARPSLLITTDDQLPRFSDVPNLT-------------------------- 573
Cdd:PRK05605 100 YAVLRLGAVVVehnPL---YTAHELEHPFEDHGARVAIVWDKVAPTVERLRRTTpletivsvnmiaampllqrlalrlpi 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 574 ---------------------SLCYNAPLTPQGSAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLL----WMQ 628
Cdd:PRK05605 177 palrkaraaltgpapgtvpweTLVDAAIGGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAqgkaWVP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 629 NHYPltGEDVVAQKTPC--SFDVSVWEFFWPFIaGAKLV-MAEPEAhrdPLAMQQFFAEygvTTTHF--VPSMLAAFVAS 703
Cdd:PRK05605 257 GLGD--GPERVLAALPMfhAYGLTLCLTLAVSI-GGELVlLPAPDI---DLILDAMKKH---PPTWLpgVPPLYEKIAEA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 704 LTPQtaRQSCATLKQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAvdvswyP-AFGEELAQVR--GSsvpIGYPVW 780
Cdd:PRK05605 328 AEER--GVDLSGVRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETS------PiIVGNPMSDDRrpGY---VGVPFP 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 781 NTGLRILDammhP------VPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADpfapgerMYRTGDVARWLDNGAVEYLG 854
Cdd:PRK05605 397 DTEVRIVD----PedpdetMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG-------WFRTGDVVVMEEDGFIRIVD 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128569 855 RSDDQLKIRGQRIELGEIDRVMQALPDVEQAVthacVINQAAATGGDarQLVGYLVSQSGLPLDTSALQAQLRETL 930
Cdd:PRK05605 466 RIKELIITGGFNVYPAEVEEVLREHPGVEDAA----VVGLPREDGSE--EVVAAVVLEPGAALDPEGLRAYCREHL 535
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
456-961 |
2.51e-24 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 109.08 E-value: 2.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 456 TLSALVAEQAAKTPDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPL 535
Cdd:PRK13382 44 GPTSGFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 536 DTGYPDDRLKMMLEDARPSLLITTD---DQLPR-FSDVP-------------NLTSLCYNAplTPQGSAPLqlSQPHHTA 598
Cdd:PRK13382 124 NTSFAGPALAEVVTREGVDTVIYDEefsATVDRaLADCPqatrivawtdedhDLTVEVLIA--AHAGQRPE--PTGRKGR 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 599 YIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTGEDVVAQKTPCsfdVSVWEFFWPFIAGAklvMAEPEAHR---DP 675
Cdd:PRK13382 200 VILLTSGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVAPM---FHAWGFSQLVLAAS---LACTIVTRrrfDP 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 676 LAMQQFFAEYGVTTTHFVPSMLAAFVASLTPQTARQSCATLKQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVDV 755
Cdd:PRK13382 274 EATLDLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAGMIA 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 756 SWYPafgeelAQVRGSSVPIGYPVWNTGLRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRpdlTASRFIadpfapgERM 835
Cdd:PRK13382 354 TATP------ADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTSG---STKDFH-------DGF 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 836 YRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQavthACVINQAAATGGDArqLVGYLVSQSGL 915
Cdd:PRK13382 418 MASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAE----AAVIGVDDEQYGQR--LAAFVVLKPGA 491
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 16128569 916 PLDTSALQAQLRETLPPHMVPVVLLQLPQLPLSANGKLDRKALPLP 961
Cdd:PRK13382 492 SATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
455-959 |
1.38e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 106.62 E-value: 1.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 455 TTLSALVAEQAAKTPDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLP 534
Cdd:PRK13383 35 TNPYTLLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 535 LDTGYPDDRLKMMLEDARPSLLITTDDQLPRFSDVPNLTSLCYNAPLTPQGSAplqlSQPHHTA---YIIFTSGSTGRPK 611
Cdd:PRK13383 115 ISTEFRSDALAAALRAHHISTVVADNEFAERIAGADDAVAVIDPATAGAEESG----GRPAVAApgrIVLLTSGTTGKPK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 612 GVmvgqtaivnrllwmqnhypltgedvvAQKTPCSFDVSVWEFFWP---FIAGAKLVMAEPEAHRDPLAMQQFFAEYG-- 686
Cdd:PRK13383 191 GV--------------------------PRAPQLRSAVGVWVTILDrtrLRTGSRISVAMPMFHGLGLGMLMLTIALGgt 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 687 -VTTTHF-------------------VPSMLAAfVASLTPQT-ARQSCATLKQVFCSGEALPADLCREWQQLTGAPLHNL 745
Cdd:PRK13383 245 vLTHRHFdaeaalaqaslhradaftaVPVVLAR-ILELPPRVrARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 746 YGPTEAAVDVSWYPafgeelAQVRGSSVPIGYPVWNTGLRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGrpdlTASRFI 825
Cdd:PRK13383 324 YGSTEVGIGALATP------ADLRDAPETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTD----GGGKAV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 826 ADPfapgerMYRTGDVArWLDN-GAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQAVthacVINQAAATGGdaRQ 904
Cdd:PRK13383 394 VDG------MTSTGDMG-YLDNaGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNA----VIGVPDERFG--HR 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 16128569 905 LVGYLVSQSGLPLDTSALQAQLRETLPPHMVPVVLLQLPQLPLSANGKLDRKALP 959
Cdd:PRK13383 461 LAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKELP 515
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
464-930 |
1.52e-23 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 105.81 E-value: 1.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 464 QAAKTPDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDR 543
Cdd:PRK03640 11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 544 LKMMLEDARPSLLITTDD--------QLPRFSDVPNLTSlcynAPLTPQGSAPLQlsqphHTAYIIFTSGSTGRPKGVMv 615
Cdd:PRK03640 91 LLWQLDDAEVKCLITDDDfeaklipgISVKFAELMNGPK----EEAEIQEEFDLD-----EVATIMYTSGTTGKPKGVI- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 616 gQTaivnrllwMQNHY----------PLTGEDvvaqktpcsfdvsVWEFFWPF--IAGAKLVMAEP--------EAHRDP 675
Cdd:PRK03640 161 -QT--------YGNHWwsavgsalnlGLTEDD-------------CWLAAVPIfhISGLSILMRSViygmrvvlVEKFDA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 676 LAMQQFFAEYGVTTTHFVPSMLAAFVASLtPQTARQScaTLKQVFCSGEalPADL-----CREWqqltGAPLHNLYGPTE 750
Cdd:PRK03640 219 EKINKLLQTGGVTIISVVSTMLQRLLERL-GEGTYPS--SFRCMLLGGG--PAPKplleqCKEK----GIPVYQSYGMTE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 751 AAVDVSWYPAfgEELAQVRGSSvpiGYPVWNTGLRILDAmMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFa 830
Cdd:PRK03640 290 TASQIVTLSP--EDALTKLGSA---GKPLFPCELKIEKD-GVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF- 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 831 pgermyRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQAVthacVINQAAATGGDARqlVGYLV 910
Cdd:PRK03640 363 ------KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAG----VVGVPDDKWGQVP--VAFVV 430
|
490 500
....*....|....*....|
gi 16128569 911 SQSGLPLDtsALQAQLRETL 930
Cdd:PRK03640 431 KSGEVTEE--ELRHFCEEKL 448
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
456-958 |
1.78e-23 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 105.87 E-value: 1.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 456 TLSALVAEQAAKTPDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPL 535
Cdd:cd05920 16 PLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 536 DTGYPDDRLKMMLEDARPSLLITtDDQLPRFSDVPNLTSLCYNAPLTpqgsAPLQLSqphhtayiiftSGSTGRPK---- 611
Cdd:cd05920 96 LPSHRRSELSAFCAHAEAVAYIV-PDRHAGFDHRALARELAESIPEV----ALFLLS-----------GGTTGTPKlipr 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 612 -----GVMVGQTAIVNRL---------LWMQNHYPLTGedvvaqktPCSFDVsvweffwpFIAGAKLVMAEPEahrDPLA 677
Cdd:cd05920 160 thndyAYNVRASAEVCGLdqdtvylavLPAAHNFPLAC--------PGVLGT--------LLAGGRVVLAPDP---SPDA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 678 MQQFFAEYGVTTTHFVPSMLAAFVASLTPQTARQSCATLKQVfcSGEALPADLCREWQQLTGAPLHNLYGPTEAAVDvsw 757
Cdd:cd05920 221 AFPLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQV--GGARLSPALARRVPPVLGCTLQQVFGMAEGLLN--- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 758 YPAFGEELAQVRGSSvpiGYPVW-NTGLRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermY 836
Cdd:cd05920 296 YTRLDDPDEVIIHTQ---GRPMSpDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF------Y 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 837 RTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVeqavthacvinQAAATGGDARQLVG-----YLVS 911
Cdd:cd05920 367 RTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAV-----------HDAAVVAMPDELLGerscaFVVL 435
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 16128569 912 QsGLPLDTSALQAQLRET-LPPHMVPVVLLQLPQLPLSANGKLDRKAL 958
Cdd:cd05920 436 R-DPPPSAAQLRRFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
446-886 |
1.92e-23 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 106.72 E-value: 1.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 446 NATQVEIPETTLSALVAEQAAKTPDAPALadaRYL-------FSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFL 518
Cdd:COG1022 2 SEFSDVPPADTLPDLLRRRAARFPDRVAL---REKedgiwqsLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 519 TLALHAIVEAGAAWLPLdtgYPDDR---LKMMLEDARPSLLIT-TDDQLPRFSDV-PNLTSL----CYNAPLTPQGSAPL 589
Cdd:COG1022 79 VIADLAILAAGAVTVPI---YPTSSaeeVAYILNDSGAKVLFVeDQEQLDKLLEVrDELPSLrhivVLDPRGLRDDPRLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 590 QLSQ----------------------PHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTGEDV--------- 638
Cdd:COG1022 156 SLDEllalgrevadpaelearraavkPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRtlsflplah 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 639 VAQKTpcsfdvsvWEFFWpFIAGAKLVMAEpeahrDPLAMQQFFAEYGVTTTHFVP----SMLAAFVASLTPQTA----- 709
Cdd:COG1022 236 VFERT--------VSYYA-LAAGATVAFAE-----SPDTLAEDLREVKPTFMLAVPrvweKVYAGIQAKAEEAGGlkrkl 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 710 ---------RQSCAT--------------------------------LKQVFCSGEALPADLCREWQQLtGAPLHNLYGP 748
Cdd:COG1022 302 frwalavgrRYARARlagkspslllrlkhaladklvfsklrealggrLRFAVSGGAALGPELARFFRAL-GIPVLEGYGL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 749 TEAAVDVS-WYPAfgeelAQVRGSsvpIGYPVWNTGLRIldammhpvppGVAGDLYLTGIQLAQGYLGRPDLTASRFIAD 827
Cdd:COG1022 381 TETSPVITvNRPG-----DNRIGT---VGPPLPGVEVKI----------AEDGEILVRGPNVMKGYYKNPEATAEAFDAD 442
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128569 828 PFapgermYRTGDVARWLDNGAVEYLGRSDDQLKIRG------QRIElgeiDRvMQALPDVEQAV 886
Cdd:COG1022 443 GW------LHTGDIGELDEDGFLRITGRKKDLIVTSGgknvapQPIE----NA-LKASPLIEQAV 496
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
463-886 |
3.51e-23 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 105.24 E-value: 3.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 463 EQAAKTPDAPAL-----ADARYLFSYREMREQVVALANLLRER-GVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLD 536
Cdd:cd05928 19 EKAGKRPPNPALwwvngKGDEVKWSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 537 TGYPDDRLKMMLEDARPSLLITTDDQLPRF----SDVPNLTSLCYNAPLTPQG----SAPLQLSQPHHTAY--------- 599
Cdd:cd05928 99 IQLTAKDILYRLQASKAKCIVTSDELAPEVdsvaSECPSLKTKLLVSEKSRDGwlnfKELLNEASTEHHCVetgsqepma 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 600 IIFTSGSTGRPKGV-----MVGQTAIVNRLLWMQnhypLTGEDVVAQKTPCSFDVSVW-EFFWPFIAGAkLVMAEPEAHR 673
Cdd:cd05928 179 IYFTSGTTGSPKMAehshsSLGLGLKVNGRYWLD----LTASDIMWNTSDTGWIKSAWsSLFEPWIQGA-CVFVHHLPRF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 674 DPLAMQQFFAEYGVTTTHFVPSMLAAFVASltpQTARQSCATLKQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAV 753
Cdd:cd05928 254 DPLVILKTLSSYPITTFCGAPTVYRMLVQQ---DLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 754 DVSWYPafGEELAQvrGSsvpIGYPVWNTGLRILDAMMHPVPPGVAGDLyltGIQLA--------QGYLGRPDLTASRFI 825
Cdd:cd05928 331 ICANFK--GMKIKP--GS---MGKASPPYDVQIIDDNGNVLPPGTEGDI---GIRVKpirpfglfSGYVDNPEKTAATIR 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128569 826 ADpfapgerMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDV-EQAV 886
Cdd:cd05928 401 GD-------FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVvESAV 455
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
457-1153 |
4.14e-23 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 106.27 E-value: 4.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 457 LSALVAEQAAKT--PDAPALAdARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAG-AAWL 533
Cdd:PRK06060 6 LAGLLAEQASEAgwYDRPAFY-AADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGvMAFL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 534 PLDTGYPDDRlKMMLEDARPSLLITTDDQLPRF--SDVPNLTSLCYNAplTPQGSAPLQLSQPHHTAYIIFTSGSTGRPK 611
Cdd:PRK06060 85 ANPELHRDDH-ALAARNTEPALVVTSDALRDRFqpSRVAEAAELMSEA--ARVAPGGYEPMGGDALAYATYTSGTTGPPK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 612 GVMVGQTAIVNRLLWM-QNHYPLTGEDVVAQKTPCSFDV----SVWeffWPFIAGAKLVMAEPEAHRDPLAMqqFFAEYG 686
Cdd:PRK06060 162 AAIHRHADPLTFVDAMcRKALRLTPEDTGLCSARMYFAYglgnSVW---FPLATGGSAVINSAPVTPEAAAI--LSARFG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 687 VTTTHFVPSMLAAFVASLTPQTARqscaTLKQVFCSGEALPADLCREWQQLTGA-PLHNLYGPTEA-------AVDvSWY 758
Cdd:PRK06060 237 PSVLYGVPNFFARVIDSCSPDSFR----SLRCVVSAGEALELGLAERLMEFFGGiPILDGIGSTEVgqtfvsnRVD-EWR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 759 PAfgeELAQVrgssvpigYPVWNtgLRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPdltasrfiaDPFAPGERMYRT 838
Cdd:PRK06060 312 LG---TLGRV--------LPPYE--IRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRP---------DSPVANEGWLDT 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 839 GDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQAlpdvEQAVTHACVINQAAATGgdARQLVGYLVSQSGLPLD 918
Cdd:PRK06060 370 RDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIE----DEAVAEAAVVAVRESTG--ASTLQAFLVATSGATID 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 919 TSALQAQLRETLP-------PHmvpvVLLQLPQLPLSANGKLDRKAlplpeLKAQAPGRAPKAGSETIIAAAFSSLLgcD 991
Cdd:PRK06060 444 GSVMRDLHRGLLNrlsafkvPH----RFAVVDRLPRTPNGKLVRGA-----LRKQSPTKPIWELSLTEPGSGVRAQR--D 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 992 VQDADADFFALGGHSLLAMKlaaqlSRQVARQVTPGQVMVASTVAKLATII-DAEEDSTRR------MGFETILPLREGN 1064
Cdd:PRK06060 513 DLSASNMTIAGGNDGGATLR-----ERLVALRQERQRLVVDAVCAEAAKMLgEPDPWSVDQdlafseLGFDSQMTVTLCK 587
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 1065 GptlfcFHPASGF------AWQF---SVLSRYLDPQWSiiGIQSpRPNGPM--QTAANLDEVCEAHLATLLEqqphgpyy 1133
Cdd:PRK06060 588 R-----LAAVTGLrlpetvGWDYgsiSGLAQYLEAELA--GGHG-RLKSAGpvNSGATGLWAIEEQLNKVEE-------- 651
|
730 740
....*....|....*....|
gi 16128569 1134 lLGYSLGGTLAQGIAARLRA 1153
Cdd:PRK06060 652 -LVAVIADGEKQRVADRLRA 670
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
481-910 |
5.93e-23 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 103.83 E-value: 5.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 481 FSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLdtgYPD---DRLKMMLEDARPSLLI 557
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPI---YPTssaEQIAYILNDSEAKALF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 558 TTDdqlprfsdvpnltslcynapltpqgsaplqlsqPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTGED 637
Cdd:cd05907 83 VED---------------------------------PDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 638 VVAQKTPCS--FDVSVWEFFwPFIAGAKLVMAEPEAhrdplAMQQFFAEYGVTTTHFVPSML----AAFVASLTPQTAR- 710
Cdd:cd05907 130 RHLSFLPLAhvFERRAGLYV-PLLAGARIYFASSAE-----TLLDDLSEVRPTVFLAVPRVWekvyAAIKVKAVPGLKRk 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 711 --QSCAT--LKQVFCSGEALPADLCREWQQLtGAPLHNLYGPTE--AAVDVSwypafgeELAQVRGSSVpiGYPVWNTGL 784
Cdd:cd05907 204 lfDLAVGgrLRFAASGGAPLPAELLHFFRAL-GIPVYEGYGLTEtsAVVTLN-------PPGDNRIGTV--GKPLPGVEV 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 785 RIldammhpvppGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermYRTGDVARWLDNGAVEYLGRSDDQLKIR- 863
Cdd:cd05907 274 RI----------ADDGEILVRGPNVMLGYYKNPEATAEALDADGW------LHTGDLGEIDEDGFLHITGRKKDLIITSg 337
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 16128569 864 GQRIELGEIDRVMQALPDVEQAVthacVInqaaatgGDARQLVGYLV 910
Cdd:cd05907 338 GKNISPEPIENALKASPLISQAV----VI-------GDGRPFLVALI 373
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
456-887 |
6.96e-23 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 106.16 E-value: 6.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 456 TLSALVAEQAAKTPDAPALADARYL-FSYREMREQVVALANLLReRGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLP 534
Cdd:PRK08633 616 PLAEAWIDTAKRNWSRLAVADSTGGeLSYGKALTGALALARLLK-RELKDEENVGILLPPSVAGALANLALLLAGKVPVN 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 535 LDTGYPDDRLKMMLEDARPSLLITT------------DDQLPRFSDV-------PNLTSL--------CYNAPLTPQGSA 587
Cdd:PRK08633 695 LNYTASEAALKSAIEQAQIKTVITSrkfleklknkgfDLELPENVKViyledlkAKISKVdkltallaARLLPARLLKRL 774
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 588 PLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTGEDVVAQKTPC--SFDVSVwEFFWPFIAGAKLV 665
Cdd:PRK08633 775 YGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFfhSFGLTV-TLWLPLLEGIKVV 853
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 666 maepeAHRDPL---AMQQFFAEYGVTTTHFVPSMLAAFVASltPQTARQSCATLKQVFCSGEALPADLCREWQQLTGAPL 742
Cdd:PRK08633 854 -----YHPDPTdalGIAKLVAKHRATILLGTPTFLRLYLRN--KKLHPLMFASLRLVVAGAEKLKPEVADAFEEKFGIRI 926
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 743 HNLYGPTE----AAVDV--SWYPAFGEELAQVRGSsvpIGYPVWNTGLRILDAM-MHPVPPGVAGDLYLTGIQLAQGYLG 815
Cdd:PRK08633 927 LEGYGATEtspvASVNLpdVLAADFKRQTGSKEGS---VGMPLPGVAVRIVDPEtFEELPPGEDGLILIGGPQVMKGYLG 1003
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128569 816 RPDLTASrFIADpfAPGERMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEI-DRVMQALPDVEQ--AVT 887
Cdd:PRK08633 1004 DPEKTAE-VIKD--IDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVeEELAKALGGEEVvfAVT 1075
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
459-891 |
4.52e-22 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 102.57 E-value: 4.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 459 ALVAEQAAKTPDAPALadaRYL--------FSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGA 530
Cdd:cd05968 65 QLLDKWLADTRTRPAL---RWEgedgtsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 531 AWLPLDTGYPDDRLKMMLEDARPSLLITTDDQLPRFSDV---PNLTSLCYNAPLT-----------PQGSAPLQLSQPH- 595
Cdd:cd05968 142 IVVPIFSGFGKEAAATRLQDAEAKALITADGFTRRGREVnlkEEADKACAQCPTVekvvvvrhlgnDFTPAKGRDLSYDe 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 596 -------HTA--------YIIFTSGSTGRPKG-VMVGQTAIVNRLLWMQNHYPLTGEDVVAQKTPCSFDVSVWEFFWPFI 659
Cdd:cd05968 222 eketagdGAErtesedplMIIYTSGTTGKPKGtVHVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMGPWLIFGGLI 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 660 AGAKLVMAE--PEaHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPQTARQSCATLKQVFCSGEAL---PADLCREW 734
Cdd:cd05968 302 LGATMVLYDgaPD-HPKADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGSTGEPWnpePWNWLFET 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 735 QQLTGAPLHNLYGPTEAAVDVswypaFG----EELAqvrgssvPIGY--PVWNTGLRILDAMMHPVPPGVaGDLYLTG-- 806
Cdd:cd05968 381 VGKGRNPIINYSGGTEISGGI-----LGnvliKPIK-------PSSFngPVPGMKADVLDESGKPARPEV-GELVLLApw 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 807 IQLAQGYLGRPDltasRFIADPFAPGERMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQAv 886
Cdd:cd05968 448 PGMTRGFWRDED----RYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLES- 522
|
....*
gi 16128569 887 thACV 891
Cdd:cd05968 523 --AAI 525
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
452-894 |
1.80e-21 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 100.80 E-value: 1.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 452 IPETTLSALvAEQAAKTPDAPAL--------ADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALP---RSVFLTL 520
Cdd:PRK07529 23 LPASTYELL-SRAAARHPDAPALsflldadpLDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPnlpETHFALW 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 521 ALHA--IV-----------------EAGAAWLPLDTGYPDDRLKMMLEDARpsllittdDQLPRFSDVPNLTSLCYNAPl 581
Cdd:PRK07529 102 GGEAagIAnpinpllepeqiaellrAAGAKVLVTLGPFPGTDIWQKVAEVL--------AALPELRTVVEVDLARYLPG- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 582 tPQGSAPLQLSQPHHTAYIIF----------------------------TSGSTGRPK------GVMVGQTAIVNRLLWm 627
Cdd:PRK07529 173 -PKRLAVPLIRRKAHARILDFdaelarqpgdrlfsgrpigpddvaayfhTGGTTGMPKlaqhthGNEVANAWLGALLLG- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 628 qnhypLTGEDVVAQKTPCsFDV--SVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFF---AEYGVTTTHFVPSMLAAFVA 702
Cdd:PRK07529 251 -----LGPGDTVFCGLPL-FHVnaLLVTGLAPLARGAHVVLATPQGYRGPGVIANFWkivERYRINFLSGVPTVYAALLQ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 703 slTPqTARQSCATLKQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVDVSWYPAFGEelaqVR-GSsvpIGYPVWN 781
Cdd:PRK07529 325 --VP-VDGHDISSLRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPDGE----RRiGS---VGLRLPY 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 782 TGLRIL-----DAMMHPVPPGVAGDLYLTGIQLAQGYLgRPDLTASRFIadpfapGERMYRTGDVARWLDNGAVEYLGRS 856
Cdd:PRK07529 395 QRVRVVilddaGRYLRDCAVDEVGVLCIAGPNVFSGYL-EAAHNKGLWL------EDGWLNTGDLGRIDADGYFWLTGRA 467
|
490 500 510
....*....|....*....|....*....|....*....
gi 16128569 857 DDqLKIR-GQRIELGEIDRVMQALPdveqAVTHACVINQ 894
Cdd:PRK07529 468 KD-LIIRgGHNIDPAAIEEALLRHP----AVALAAAVGR 501
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
456-884 |
2.65e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 99.85 E-value: 2.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 456 TLSALVAEQAAKTPDAPALA----DARYlfSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAA 531
Cdd:PRK12583 19 TIGDAFDATVARFPDREALVvrhqALRY--TWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 532 WLPLDTGYPDDRLKMMLEDARPSLLITTD-----------DQL--------------PRFSDVPNLTSLCYNAP------ 580
Cdd:PRK12583 97 LVNINPAYRASELEYALGQSGVRWVICADafktsdyhamlQELlpglaegqpgalacERLPELRGVVSLAPAPPpgflaw 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 581 ---------LTPQGSAPLQLS-QPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTGEDVVAQKTPcsfdvs 650
Cdd:PRK12583 177 helqargetVSREALAERQASlDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVP------ 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 651 VWEFFWPFIA-------GAKLVMaePEAHRDPLAMQQFFAEYGVTTTHFVPSMlaaFVASLT-PQTARQSCATLKQVFCS 722
Cdd:PRK12583 251 LYHCFGMVLAnlgcmtvGACLVY--PNEAFDPLATLQAVEEERCTALYGVPTM---FIAELDhPQRGNFDLSSLRTGIMA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 723 GEALPADLCRE-WQQLTGAPLHNLYGPTEAAvDVSWYPAFGEELaQVRGSSVPIGYPvwNTGLRILDAMMHPVPPGVAGD 801
Cdd:PRK12583 326 GAPCPIEVMRRvMDEMHMAEVQIAYGMTETS-PVSLQTTAADDL-ERRVETVGRTQP--HLEVKVVDPDGATVPRGEIGE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 802 LYLTGIQLAQGYLGRPDLTASRFIADPFapgerMYrTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPD 881
Cdd:PRK12583 402 LCTRGYSVMKGYWNNPEATAESIDEDGW-----MH-TGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPA 475
|
...
gi 16128569 882 VEQ 884
Cdd:PRK12583 476 VAD 478
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
456-885 |
5.92e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 98.47 E-value: 5.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 456 TLSALVAEQAAKTPDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAvALPRS--VFLTLALhAIVEAGAAWL 533
Cdd:PRK08316 12 TIGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVA-ALGHNsdAYALLWL-ACARAGAVHV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 534 PLDTGYPDDRLKMMLEDARPSLLITTDDQLPRFSDVPNLTSLCYN--APLTPQGSAP--------LQLSQPHHT------ 597
Cdd:PRK08316 90 PVNFMLTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLilSLVLGGREAPggwldfadWAEAGSVAEpdvela 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 598 ----AYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTGEDVVAQKTP---CS-FDVsvweFFWPFIA-GAK-LVMA 667
Cdd:PRK08316 170 dddlAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPlyhCAqLDV----FLGPYLYvGATnVILD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 668 EPeahrDPLAMQQFFAEYGVTTTHFVPSMLAAFVASltPQTARQSCATLKQVFCSGEALPADLCREWQQ-LTGAPLHNLY 746
Cdd:PRK08316 246 AP----DPELILRTIEAERITSFFAPPTVWISLLRH--PDFDTRDLSSLRKGYYGASIMPVEVLKELRErLPGLRFYNCY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 747 GPTEAAvdvswyP---AFGEELAQVRGSSVpiGYPVWNTGLRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASR 823
Cdd:PRK08316 320 GQTEIA------PlatVLGPEEHLRRPGSA--GRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEA 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128569 824 FIADPFapgermyRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQA 885
Cdd:PRK08316 392 FRGGWF-------HSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEV 446
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
598-958 |
7.02e-21 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 95.48 E-value: 7.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 598 AYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTGEDVVAQKTPcSFDVSVWEFFWP-FIAGAKLVMAEPEAhrdpl 676
Cdd:cd17630 3 ATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLP-LYHVGGLAILVRsLLAGAELVLLERNQ----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 677 AMQQFFAEYGVTTTHFVPSMLAAFVASLTPQTARqscATLKQVFCSGEALPADLCREWQQLtGAPLHNLYGPTEAAVDVS 756
Cdd:cd17630 77 ALAEDLAPPGVTHVSLVPTQLQRLLDSGQGPAAL---KSLRAVLLGGAPIPPELLERAADR-GIPLYTTYGMTETASQVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 757 WYPAFGEELAQVrgssvpiGYPVWNTGLRILDAmmhpvppgvaGDLYLTGIQLAQGYLGRPdltasrfIADPFaPGERMY 836
Cdd:cd17630 153 TKRPDGFGRGGV-------GVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQ-------LVPEF-NEDGWF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 837 RTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQavthACVINQAAATGGdaRQLVGYLVSQSglP 916
Cdd:cd17630 208 TTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRD----AFVVGVPDEELG--QRPVAVIVGRG--P 279
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 16128569 917 LDTSALQAQLRETLPPHMVPVVLLQLPQLPLSANGKLDRKAL 958
Cdd:cd17630 280 ADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
474-893 |
1.38e-20 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 97.17 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 474 LADARYLF-SYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDR----LKMML 548
Cdd:cd05908 8 LGDKKEKFvSYRHLREEALGYLGALQELGIKPGQEVVFQITHNNKFLYLFWACLLGGMIAVPVSIGSNEEHklklNKVWN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 549 EDARPsLLITTDDQLPRFSDvpnltslcynapltpqgsaplqlsqphHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQ 628
Cdd:cd05908 88 TLKNP-YLITEEEVLCELAD---------------------------ELAFIQFSSGSTGDPKGVMLTHENLVHNMFAIL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 629 NHYPLTGEDVVAQKTPCSFDVSVWEF-FWPFIAGAK-LVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTP 706
Cdd:cd05908 140 NSTEWKTKDRILSWMPLTHDMGLIAFhLAPLIAGMNqYLMPTRLFIRRPILWLKKASEHKATIVSSPNFGYKYFLKTLKP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 707 QTARQ-SCATLKQVFCSGEALPADLCREWQQ------LTGAPLHNLYGPTEAAVDVSWYPA---------------FGEE 764
Cdd:cd05908 220 EKANDwDLSSIRMILNGAEPIDYELCHEFLDhmskygLKRNAILPVYGLAEASVGASLPKAqspfktitlgrrhvtHGEP 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 765 LAQVRGSS------VPIGYPVWNTGLRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermYRT 838
Cdd:cd05908 300 EPEVDKKDsecltfVEVGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGW------LKT 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 16128569 839 GDVArWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQAVTHACVIN 893
Cdd:cd05908 374 GDLG-FIRNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVELGRVVACGVN 427
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
457-928 |
1.73e-20 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 96.98 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 457 LSALVAEQAAktPDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAwlPLD 536
Cdd:PRK10946 27 LTDILTRHAA--SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA--PVN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 537 TGYPDDRLKMmLEDAR---PSLLITtDDQLPRFSDVPNLTSLCYNAP--------------------LTPQGSAPLQLSQ 593
Cdd:PRK10946 103 ALFSHQRSEL-NAYASqiePALLIA-DRQHALFSDDDFLNTLVAEHSslrvvlllnddgehslddaiNHPAEDFTATPSP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 594 PHHTAYIIFTSGSTGRPKGV-------------------MVGQTAIVNRLLWMQNhYPLTgedvvaqkTPCSFDVsvwef 654
Cdd:PRK10946 181 ADEVAFFQLSGGSTGTPKLIprthndyyysvrrsveicgFTPQTRYLCALPAAHN-YPMS--------SPGALGV----- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 655 fwpFIAGAKLVMAepeahRDPLAMQQF--FAEYGVTTTHFVPSMLAAFVASLTPQTARQSCATLKQVFCSGEALPADLCR 732
Cdd:PRK10946 247 ---FLAGGTVVLA-----PDPSATLCFplIEKHQVNVTALVPPAVSLWLQAIAEGGSRAQLASLKLLQVGGARLSETLAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 733 EWQQLTGAPLHNLYGPTEAAVDvswYPAFGEELAQVRGSSvpiGYPVW-NTGLRILDAMMHPVPPGVAGDLYLTGIQLAQ 811
Cdd:PRK10946 319 RIPAELGCQLQQVFGMAEGLVN---YTRLDDSDERIFTTQ---GRPMSpDDEVWVADADGNPLPQGEVGRLMTRGPYTFR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 812 GYLGRPDLTASRFIADPFapgermYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPdveqAVTHACV 891
Cdd:PRK10946 393 GYYKSPQHNASAFDANGF------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHP----AVIHAAL 462
|
490 500 510
....*....|....*....|....*....|....*..
gi 16128569 892 INQAAATGGDarQLVGYLVSQSglPLDTSALQAQLRE 928
Cdd:PRK10946 463 VSMEDELMGE--KSCAFLVVKE--PLKAVQLRRFLRE 495
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
482-958 |
4.86e-20 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 94.34 E-value: 4.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 482 SYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLlittDD 561
Cdd:cd05912 3 TFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL----DD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 562 qlprfsdvpnltslcynapltpqgsaplqlsqphhTAYIIFTSGSTGRPKGVMvgQTAivnrllwmQNHYpltgEDVVAQ 641
Cdd:cd05912 79 -----------------------------------IATIMYTSGTTGKPKGVQ--QTF--------GNHW----WSAIGS 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 642 KTPCSF-DVSVWEFFWPF--IAGAKLVM--------AEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLAafvaSLTPQTAR 710
Cdd:cd05912 110 ALNLGLtEDDNWLCALPLfhISGLSILMrsviygmtVYLVDKFDAEQVLHLINSGKVTIISVVPTMLQ----RLLEILGE 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 711 QSCATLKQVFCSGEALPADLCREWQQLtGAPLHNLYGPTEAAvdvSWYPAFGEELAQVRGSSVpiGYPVWNTGLRILDAM 790
Cdd:cd05912 186 GYPNNLRCILLGGGPAPKPLLEQCKEK-GIPVYQSYGMTETC---SQIVTLSPEDALNKIGSA--GKPLFPVELKIEDDG 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 791 mhpVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermyRTGDVArWLDN-GAVEYLGRSDDQLKIRGQRIEL 869
Cdd:cd05912 260 ---QPPYEVGEILLKGPNVTKGYLNRPDATEESFENGWF-------KTGDIG-YLDEeGFLYVLDRRSDLIISGGENIYP 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 870 GEIDRVMQALPDVEQAVthacVINQAAATGGdarQL-VGYLVSQSglPLDTSALQAQLRETLPPHMVPVVLLQLPQLPLS 948
Cdd:cd05912 329 AEIEEVLLSHPAIKEAG----VVGIPDDKWG---QVpVAFVVSER--PISEEELIAYCSEKLAKYKVPKKIYFVDELPRT 399
|
490
....*....|
gi 16128569 949 ANGKLDRKAL 958
Cdd:cd05912 400 ASGKLLRHEL 409
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
445-958 |
7.53e-20 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 94.87 E-value: 7.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 445 LNATQVEIPETTLSA--LVAEQAAKTPDAPALA---DA--RYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSV- 516
Cdd:cd05970 5 HNNFSINVPENFNFAydVVDAMAKEYPDKLALVwcdDAgeERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYe 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 517 --FLTLALHAI----VEAGAAWLPLDTGYPDDR--LKMMLEDARPSLLITTDDQLPrfsDVPNLTSLCYNAPLTPQG--- 585
Cdd:cd05970 85 fwYSLLALHKLgaiaIPATHQLTAKDIVYRIESadIKMIVAIAEDNIPEEIEKAAP---ECPSKPKLVWVGDPVPEGwid 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 586 ------SAPLQLSQPHHTAY--------IIFTSGSTGRPKGVMVGQT----AIVNRLLWmQNHYP----LTGEDVVAQKt 643
Cdd:cd05970 162 frklikNASPDFERPTANSYpcgedillVYFSSGTTGMPKMVEHDFTyplgHIVTAKYW-QNVREgglhLTVADTGWGK- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 644 pcsfdvSVW-EFFWPFIAGAKLVMAEPEAHrDPLAMQQFFAEYGVTTTHFVPSMLAAFV-ASLTpqtaRQSCATLKQVFC 721
Cdd:cd05970 240 ------AVWgKIYGQWIAGAAVFVYDYDKF-DPKALLEKLSKYGVTTFCAPPTIYRFLIrEDLS----RYDLSSLRYCTT 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 722 SGEALPADLCREWQQLTGAPLHNLYGPTEAAVDVSWYPAfgeeLAQVRGSsvpIGYPVWNTGLRILDAMMHPVPPGVAGD 801
Cdd:cd05970 309 AGEALNPEVFNTFKEKTGIKLMEGFGQTETTLTIATFPW----MEPKPGS---MGKPAPGYEIDLIDREGRSCEAGEEGE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 802 LYL-----TGIQLAQGYLGRPDLTASRFiadpfapGERMYRTGDVArWLD-NGAVEYLGRSDDQLKIRGQRIELGEIDRV 875
Cdd:cd05970 382 IVIrtskgKPVGLFGGYYKDAEKTAEVW-------HDGYYHTGDAA-WMDeDGYLWFVGRTDDLIKSSGYRIGPFEVESA 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 876 MQALPDV-EQAVTHAC--VINQAA-ATGGDARqlvGYLVSQSglplDTSALQAQLRETLPPHMVPVVLLQLPQLPLSANG 951
Cdd:cd05970 454 LIQHPAVlECAVTGVPdpIRGQVVkATIVLAK---GYEPSEE----LKKELQDHVKKVTAPYKYPRIVEFVDELPKTISG 526
|
....*..
gi 16128569 952 KLDRKAL 958
Cdd:cd05970 527 KIRRVEI 533
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
457-958 |
2.57e-19 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 93.41 E-value: 2.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 457 LSALVAEQAAKTPDAPAL--ADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLP 534
Cdd:PRK05852 18 IADLVEVAATRLPEAPALvvTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 535 LDTGYP--DDRLKMMLEDARPSLL---------------------ITTDDQLPRFSDVPNLTSlcyNAPLTPQGSAPLQL 591
Cdd:PRK05852 98 LDPALPiaEQRVRSQAAGARVVLIdadgphdraepttrwwpltvnVGGDSGPSGGTLSVHLDA---ATEPTPATSTPEGL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 592 SqpHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTGEDVVAQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEA 671
Cdd:PRK05852 175 R--PDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLPARG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 672 HRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPQTARQSCATLKQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEA 751
Cdd:PRK05852 253 RFSAHTFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKPAALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 752 AVDVSWYPAFGeeLAQVRGSSVPIGYPVWNTG--LRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIadpf 829
Cdd:PRK05852 333 THQVTTTQIEG--IGQTENPVVSTGLVGRSTGaqIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFT---- 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 830 apgERMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQAVthacVINQAAATGGDARQLVgyL 909
Cdd:PRK05852 407 ---DGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAA----VFGVPDQLYGEAVAAV--I 477
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 16128569 910 VSQSGLPLDTSALQAQLRETLPPHMVPVVLLQLPQLPLSANGKLDRKAL 958
Cdd:PRK05852 478 VPRESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAV 526
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
466-958 |
4.51e-19 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 92.60 E-value: 4.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 466 AKTPDAPALADARYLF--SYREMREQVVALANLLRER-GVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDD 542
Cdd:PLN02574 50 HNHNGDTALIDSSTGFsiSYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 543 RLKMMLEDARPSLLITTDDQLPRFSD-------VPNLTSLCYNAPLTPQ---------GSAPLQLSQPHHTAYIIFTSGS 606
Cdd:PLN02574 130 EIKKRVVDCSVGLAFTSPENVEKLSPlgvpvigVPENYDFDSKRIEFPKfyelikedfDFVPKPVIKQDDVAAIMYSSGT 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 607 TGRPKGVMVGQTAIVN------RLLWMQNHYPLTGEDVVAQKTPCS-FDVSVWEFFWPFIAGAKLVMAEPEAHRdplaMQ 679
Cdd:PLN02574 210 TGASKGVVLTHRNLIAmvelfvRFEASQYEYPGSDNVYLAALPMFHiYGLSLFVVGLLSLGSTIVVMRRFDASD----MV 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 680 QFFAEYGVTttHF--VPSMLAAFVasltpQTARQSCA----TLKQVFCSGEALPADLCREW-QQLTGAPLHNLYGPTE-A 751
Cdd:PLN02574 286 KVIDRFKVT--HFpvVPPILMALT-----KKAKGVCGevlkSLKQVSCGAAPLSGKFIQDFvQTLPHVDFIQGYGMTEsT 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 752 AVDVSwypAFGEELAQvRGSSVPIGYPvwNTGLRILDAMMHP-VPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFa 830
Cdd:PLN02574 359 AVGTR---GFNTEKLS-KYSSVGLLAP--NMQAKVVDWSTGClLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGW- 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 831 pgermYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIelgeidrvmqALPDVEQAVTHACVINQAAATGGDARQL----V 906
Cdd:PLN02574 432 -----LRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQI----------APADLEAVLISHPEIIDAAVTAVPDKECgeipV 496
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 16128569 907 GYLVSQSGLPLDTSALQAQLRETLPPHMVPVVLLQLPQLPLSANGKLDRKAL 958
Cdd:PLN02574 497 AFVVRRQGSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRREL 548
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
481-905 |
4.71e-19 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 92.04 E-value: 4.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 481 FSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTD 560
Cdd:cd17640 6 ITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVVEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 561 DqlprfsdvpnltslcynapltpqgsaplqlsqPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTGEDVVA 640
Cdd:cd17640 86 D--------------------------------SDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 641 QKTPC--SFDVSVWEFFwpFIAGAKLVMAEPEAHRDPLamQQFFAEYGVTtthfVPSMLAAFVASLTPQTARQScATLKQ 718
Cdd:cd17640 134 SILPIwhSYERSAEYFI--FACGCSQAYTSIRTLKDDL--KRVKPHYIVS----VPRLWESLYSGIQKQVSKSS-PIKQF 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 719 VF-------------CSGEALPADLCReWQQLTGAPLHNLYGPTEAAVDVSwypaFGEELAQVRGSsvpIGYPVWNTGLR 785
Cdd:cd17640 205 LFlfflsggifkfgiSGGGALPPHVDT-FFEAIGIEVLNGYGLTETSPVVS----ARRLKCNVRGS---VGRPLPGTEIK 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 786 ILDAMMH-PVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermYRTGDVARWLDNGAVEYLGRSDDQLKIR- 863
Cdd:cd17640 277 IVDPEGNvVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW------FNTGDLGWLTCGGELVLTGRAKDTIVLSn 350
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 16128569 864 GQRIELGEIdrvmqalpdvEQAVTHACVINQAAATGGDARQL 905
Cdd:cd17640 351 GENVEPQPI----------EEALMRSPFIEQIMVVGQDQKRL 382
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
457-926 |
6.03e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 92.03 E-value: 6.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 457 LSALVAEQAAKTPDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLD 536
Cdd:PRK07470 9 LAHFLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 537 TGYPDDRLKMMLEDARPSLLITTDD----------QLPRFSDVPNL----TSLCYNAPLTPQGSAPLQLSQPHHT--AYI 600
Cdd:PRK07470 89 FRQTPDEVAYLAEASGARAMICHADfpehaaavraASPDLTHVVAIggarAGLDYEALVARHLGARVANAAVDHDdpCWF 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 601 IFTSGSTGRPKGVMV--GQTAIVnrllwMQNH----YPLTGED----VVAqktPCSFDVSVWEFFwPFIAGAKLVMAePE 670
Cdd:PRK07470 169 FFTSGTTGRPKAAVLthGQMAFV-----ITNHladlMPGTTEQdaslVVA---PLSHGAGIHQLC-QVARGAATVLL-PS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 671 AHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASltPQTARQSCATLKQVFCSGealpADLCREWQQLT----GAPLHNLY 746
Cdd:PRK07470 239 ERFDPAEVWALVERHRVTNLFTVPTILKMLVEH--PAVDRYDHSSLRYVIYAG----APMYRADQKRAlaklGKVLVQYF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 747 GPTEAAVDVSWYPAFGEELAQVRGSSV-PIGYPvwNTG--LRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASR 823
Cdd:PRK07470 313 GLGEVTGNITVLPPALHDAEDGPDARIgTCGFE--RTGmeVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 824 FIADPFapgermyRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPdveqAVTHACVINQAAATGGDAR 903
Cdd:PRK07470 391 FRDGWF-------RTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHP----AVSEVAVLGVPDPVWGEVG 459
|
490 500
....*....|....*....|...
gi 16128569 904 qlVGYLVSQSGLPLDTSALQAQL 926
Cdd:PRK07470 460 --VAVCVARDGAPVDEAELLAWL 480
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
597-955 |
6.96e-19 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 89.63 E-value: 6.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 597 TAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNH-YPLTGEDVVAQKTPCSFDVSVWEFFWPFIAGAKLVMAepeahRDP 675
Cdd:cd17635 3 PLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEgLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTG-----GEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 676 LAMQQFFAE---YGVTTTHFVPSMLAAFVASLTpqTARQSCATLKQVFCSGEALPADLCR--EWQQLTGAPLHnlYGPTE 750
Cdd:cd17635 78 TTYKSLFKIlttNAVTTTCLVPTLLSKLVSELK--SANATVPSLRLIGYGGSRAIAADVRfiEATGLTNTAQV--YGLSE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 751 aaVDVSWYPAFGEELAQVRGssvpIGYPVWNTGLRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIadpfa 830
Cdd:cd17635 154 --TGTALCLPTDDDSIEINA----VGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI----- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 831 pgERMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQAvthACvinqAAATGGDARQLVGYLV 910
Cdd:cd17635 223 --DGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQEC---AC----YEISDEEFGELVGLAV 293
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 16128569 911 SQSGLpLDTSALQAQ---LRETLPPHMVPVVLLQLPQLPLSANGKLDR 955
Cdd:cd17635 294 VASAE-LDENAIRALkhtIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
455-887 |
7.11e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 91.20 E-value: 7.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 455 TTLSALVAEQAAKTPDAPALADAryLFSYREMREQVVALAnllrERgVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLP 534
Cdd:PRK07787 2 ASLNPAAVAAAADIADAVRIGGR--VLSRSDLAGAATAVA----ER-VAGARRVAVLATPTLATVLAVVGALIAGVPVVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 535 L--DTGypDDRLKMMLEDARPSL-LITTDDQLPRFSDVPnltslcynAPLTPQGSAPLQLSQPHHTAYIIFTSGSTGRPK 611
Cdd:PRK07787 75 VppDSG--VAERRHILADSGAQAwLGPAPDDPAGLPHVP--------VRLHARSWHRYPEPDPDAPALIVYTSGTTGPPK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 612 GVMVGQTAIVNRLLWMQNHYPLTGEDVVAQKTPCsFDVS--VWEFFWPFIAGAKLV-MAEPeahrDPLAMQQffAEYGVT 688
Cdd:PRK07787 145 GVVLSRRAIAADLDALAEAWQWTADDVLVHGLPL-FHVHglVLGVLGPLRIGNRFVhTGRP----TPEAYAQ--ALSEGG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 689 TTHF-VPSMLAAFVASltPQTARQ-SCATLkqvFCSGEA-LPADLCREWQQLTGAPLHNLYGPTEAAVDVSwypafgeel 765
Cdd:PRK07787 218 TLYFgVPTVWSRIAAD--PEAARAlRGARL---LVSGSAaLPVPVFDRLAALTGHRPVERYGMTETLITLS--------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 766 AQVRGSSVP--IGYPVWNTGLRILDAMMHPVPPGVA--GDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermYRTGDV 841
Cdd:PRK07787 284 TRADGERRPgwVGLPLAGVETRLVDEDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGW------FRTGDV 357
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 16128569 842 ARWLDNGAVEYLGR-SDDQLKIRGQRIELGEIDRVMQALPDV-EQAVT 887
Cdd:PRK07787 358 AVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHPGVrEAAVV 405
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
456-886 |
8.80e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 91.49 E-value: 8.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 456 TLSALVAEQAAKTPDAPAL--ADARYlfSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWL 533
Cdd:PRK07798 4 NIADLFEAVADAVPDRVALvcGDRRL--TYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 534 PLDTGYPDDRLKMMLEDARPSLLITTDDQLPRFSDV-PNLTSLCY---------NAPLTP---------QGSAPLQLSQP 594
Cdd:PRK07798 82 NVNYRYVEDELRYLLDDSDAVALVYEREFAPRVAEVlPRLPKLRTlvvvedgsgNDLLPGavdyedalaAGSPERDFGER 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 595 hhTA---YIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHY----PLTGEDVVAQKTPCSFDV-----------SVWEFFW 656
Cdd:PRK07798 162 --SPddlYLLYTGGTTGMPKGVMWRQEDIFRVLLGGRDFAtgepIEDEEELAKRAAAGPGMRrfpapplmhgaGQWAAFA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 657 PFIAGAKLVMaEPEAHRDPLAMQQFFAEYGVTTTHFV------PsMLAAFVAsltpqTARQSCATLKQVFCSGEALPADL 730
Cdd:PRK07798 240 ALFSGQTVVL-LPDVRFDADEVWRTIEREKVNVITIVgdamarP-LLDALEA-----RGPYDLSSLFAIASGGALFSPSV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 731 CREWQ-QLTGAPLHNLYGPTEAAVDVSWYPAFGEelaqvrgssVPIGYPVWNTGLR--ILDAMMHPVPPG--VAGDLYLT 805
Cdd:PRK07798 313 KEALLeLLPNVVLTDSIGSSETGFGGSGTVAKGA---------VHTGGPRFTIGPRtvVLDEDGNPVEPGsgEIGWIARR 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 806 GiQLAQGYLGRPDLTASRFiadPFAPGERMYRTGDVARWLDNGAVEYLGRsdDQLKIR--GQRIELGEIDRVMQALPDVE 883
Cdd:PRK07798 384 G-HIPLGYYKDPEKTAETF---PTIDGVRYAIPGDRARVEADGTITLLGR--GSVCINtgGEKVFPEEVEEALKAHPDVA 457
|
...
gi 16128569 884 QAV 886
Cdd:PRK07798 458 DAL 460
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
603-931 |
1.01e-18 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 89.46 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 603 TSGSTGRPKgvmVGQTAIVNRLL--WMQNHYPLTGEDVVAQKTPCSFDV--SVWEFFWPFIAGAKLVMAEPEAHRDPLAM 678
Cdd:cd05944 10 TGGTTGTPK---LAQHTHSNEVYnaWMLALNSLFDPDDVLLCGLPLFHVngSVVTLLTPLASGAHVVLAGPAGYRNPGLF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 679 QQFF---AEYGVTTTHFVPSMLAAFVAslTPQTARQScaTLKQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVDV 755
Cdd:cd05944 87 DNFWklvERYRITSLSTVPTVYAALLQ--VPVNADIS--SLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 756 SWYPAFGEElaqvRGSSVPIGYPVWNTGLRILDAMMH---PVPPGVAGDLYLTGIQLAQGYLgRPDLTASRFIADpfapg 832
Cdd:cd05944 163 AVNPPDGPK----RPGSVGLRLPYARVRIKVLDGVGRllrDCAPDEVGEICVAGPGVFGGYL-YTEGNKNAFVAD----- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 833 eRMYRTGDVARWLDNGAVEYLGRSDDqLKIR-GQRIELGEIDRVMQALPdveqAVTHACVINQAAATGGDARqlVGYLVS 911
Cdd:cd05944 233 -GWLNTGDLGRLDADGYLFITGRAKD-LIIRgGHNIDPALIEEALLRHP----AVAFAGAVGQPDAHAGELP--VAYVQL 304
|
330 340
....*....|....*....|
gi 16128569 912 QSGLPLDTSALQAQLRETLP 931
Cdd:cd05944 305 KPGAVVEEEELLAWARDHVP 324
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
482-930 |
1.21e-18 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 90.91 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 482 SYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTDD 561
Cdd:PRK12406 13 SFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHAD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 562 QL-PRFSDVP-NLTSLCYNAP--------------LTPQG-------------SAPLQLSQPhhtAYIIFTSGSTGRPKG 612
Cdd:PRK12406 93 LLhGLASALPaGVTVLSVPTPpeiaaayrispallTPPAGaidwegwlaqqepYDGPPVPQP---QSMIYTSGTTGHPKG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 613 V-----MVGQTAIvnrllWMQNHYPLTG--EDVVAQKT-------PCSFDVSVWEFfwpfiaGAKLVMaepEAHRDPLAM 678
Cdd:PRK12406 170 VrraapTPEQAAA-----AEQMRALIYGlkPGIRALLTgplyhsaPNAYGLRAGRL------GGVLVL---QPRFDPEEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 679 QQFFAEYGVTTTHFVPSMLAAFVASLTPQTARQSCATLKQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVdVSWy 758
Cdd:PRK12406 236 LQLIERHRITHMHMVPTMFIRLLKLPEEVRAKYDVSSLRHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTESGA-VTF- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 759 pAFGEELAQVRGSsvpIGYPVWNTGLRILDAMMHPVPPGVAGDLYLTGIQLAQ-GYLGRPDLTAS----RFIAdpfapge 833
Cdd:PRK12406 314 -ATSEDALSHPGT---VGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAEidrgGFIT------- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 834 rmyrTGDVArWLD-NGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVeqavtHAC-VINQAAATGGDArqLVGYLVS 911
Cdd:PRK12406 383 ----SGDVG-YLDaDGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGV-----HDCaVFGIPDAEFGEA--LMAVVEP 450
|
490
....*....|....*....
gi 16128569 912 QSGLPLDTSALQAQLRETL 930
Cdd:PRK12406 451 QPGATLDEADIRAQLKARL 469
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
461-886 |
2.28e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 90.22 E-value: 2.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 461 VAEQAAKTPDAPALadaRYL---FSYREMREQVVALANLLRERGVKPGDSVAV-ALPRSVFLTLALhAIVEAGAAWLPLD 536
Cdd:PRK07786 23 LARHALMQPDAPAL---RFLgntTTWRELDDRVAALAGALSRRGVGFGDRVLIlMLNRTEFVESVL-AANMLGAIAVPVN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 537 TGYPDDRLKMMLEDARPSLLITTDDQLPRFS----DVPNL------------TSLCYNAPLTPQGSAPLQLSQPHHT-AY 599
Cdd:PRK07786 99 FRLTPPEIAFLVSDCGAHVVVTEAALAPVATavrdIVPLLstvvvaggssddSVLGYEDLLAEAGPAHAPVDIPNDSpAL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 600 IIFTSGSTGRPKGVMVGQTAIVNRLLWM--QNHYPlTGEDVVAQKTPCSFDVSVWEFFWPFIAGAKLVMaEPEAHRDPLA 677
Cdd:PRK07786 179 IMYTSGTTGRPKGAVLTHANLTGQAMTClrTNGAD-INSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVI-YPLGAFDPGQ 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 678 MQQFFAEYGVTTTHFVPsmlAAFVASLTPQTARQSCATLKqvFCSGEALPAD--LCRE-WQQLTGAPLHNLYGPTEAAvd 754
Cdd:PRK07786 257 LLDVLEAEKVTGIFLVP---AQWQAVCAEQQARPRDLALR--VLSWGAAPASdtLLRQmAATFPEAQILAAFGQTEMS-- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 755 vswyPA----FGEELAQVRGSsvpIGYPVWNTGLRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTasrfiADPFA 830
Cdd:PRK07786 330 ----PVtcmlLGEDAIRKLGS---VGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEAT-----AEAFA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 16128569 831 PGerMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPD-VEQAV 886
Cdd:PRK07786 398 GG--WFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDiVEVAV 452
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
481-885 |
2.59e-18 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 89.16 E-value: 2.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 481 FSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEdaRPSLLITTD 560
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVD--RGGAVYAAV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 561 DQLPRFSDvpnltslcynapltpqgsaPLQLsqphhtayiIFTSGSTGRPKGVMVGQTAI----VNRLLWMQnhypLTGE 636
Cdd:cd05974 79 DENTHADD-------------------PMLL---------YFTSGTTSKPKLVEHTHRSYpvghLSTMYWIG----LKPG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 637 DVVAQKTPCSFDVSVWE-FFWPFIAGAKlVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVasltpQTARQSCAT 715
Cdd:cd05974 127 DVHWNISSPGWAKHAWScFFAPWNAGAT-VFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLI-----QQDLASFDV 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 716 -LKQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVDVSWYPafGEELaqVRGSsvpIGYPVWNTGLRILDAMMHPV 794
Cdd:cd05974 201 kLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSP--GQPV--KAGS---MGRPLPGYRVALLDPDGAPA 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 795 PPG-VAGDLYLT-GIQLAQGYLGRPDLTASrfiadpfAPGERMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEI 872
Cdd:cd05974 274 TEGeVALDLGDTrPVGLMKGYAGDPDKTAH-------AMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFEL 346
|
410
....*....|...
gi 16128569 873 DRVMQALPDVEQA 885
Cdd:cd05974 347 ESVLIEHPAVAEA 359
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
482-855 |
7.56e-18 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 87.90 E-value: 7.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 482 SYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITtdd 561
Cdd:cd05910 4 SFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFIG--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 562 qLPRFSDvpnltslcynapltpqgsaplqlsqphhTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTGEDVvaq 641
Cdd:cd05910 81 -IPKADE----------------------------PAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEV--- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 642 ktpcsfDVSVWEFFWPFIAGAKLVMAEPE------AHRDPLAMQQFFAEYGVTTTHFVPSMLAAfVASLTPQTARQsCAT 715
Cdd:cd05910 129 ------DLATFPLFALFGPALGLTSVIPDmdptrpARADPQKLVGAIRQYGVSIVFGSPALLER-VARYCAQHGIT-LPS 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 716 LKQVFCSGEALPADLCREWQQLT--GAPLHNLYGPTEA----AVDVSWYPAFGEELAQvRGSSVPIGYPVWNTGLRILDA 789
Cdd:cd05910 201 LRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEAlpvsSIGSRELLATTTAATS-GGAGTCVGRPIPGVRVRIIEI 279
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128569 790 ---------MMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADpfaPGERM-YRTGDVARWLDNGAVEYLGR 855
Cdd:cd05910 280 ddepiaewdDTLELPRGEIGEITVTGPTVTPTYVNRPVATALAKIDD---NSEGFwHRMGDLGYLDDEGRLWFCGR 352
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
456-882 |
7.65e-18 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 88.78 E-value: 7.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 456 TLSALVAEQAAKTPDAPALADARYLFSYREMREQVVALAN-LLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLP 534
Cdd:PRK08751 26 TVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAyLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 535 LDTGYPDDRLKMMLEDARPSLLITTDDQLPRFSDVPNLTS------------------------LCYNAPLTP------- 583
Cdd:PRK08751 106 VNPLYTPRELKHQLIDSGASVLVVIDNFGTTVQQVIADTPvkqvittglgdmlgfpkaalvnfvVKYVKKLVPeyringa 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 584 -----------QGSAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLL----WMQNHYPLT-GEDVVAQKTPCS- 646
Cdd:PRK08751 186 irfrealalgrKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQqahqWLAGTGKLEeGCEVVITALPLYh 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 647 -FDVSVWEFFWPFIAGAKLVMAEPeahRDplaMQQFFAEYGVTTTHFVPSMLAAFVASL-TPQTARQSCATLKQVFCSGE 724
Cdd:PRK08751 266 iFALTANGLVFMKIGGCNHLISNP---RD---MPGFVKELKKTRFTAFTGVNTLFNGLLnTPGFDQIDFSSLKMTLGGGM 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 725 ALPADLCREWQQLTGAPLHNLYGPTEAAVDVSWYPAfgeELAQVRGSsvpIGYPVWNTGLRILDAMMHPVPPGVAGDLYL 804
Cdd:PRK08751 340 AVQRSVAERWKQVTGLTLVEAYGLTETSPAACINPL---TLKEYNGS---IGLPIPSTDACIKDDAGTVLAIGEIGELCI 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128569 805 TGIQLAQGYLGRPDLTASRFIADPFapgermYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDV 882
Cdd:PRK08751 414 KGPQVMKGYWKRPEETAKVMDADGW------LHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGV 485
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
455-928 |
9.13e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 88.20 E-value: 9.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 455 TTLSALVAEQAAKtpDAPALADARYLFSYREMREQVVALANLLRER--GVKPGdSVAVALPRSVFLTLALHAIVEAGAAW 532
Cdd:PRK07867 5 PTVAELLLPLAED--DDRGLYFEDSFTSWREHIRGSAARAAALRARldPTRPP-HVGVLLDNTPEFSLLLGAAALSGIVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 533 LPLDTGYPDDRLKMMLEDARPSLLITTDDQLPRFSDVP------NLTSLCYNAPLTPQGSAPLQLS--QPHHTAYIIFTS 604
Cdd:PRK07867 82 VGLNPTRRGAALARDIAHADCQLVLTESAHAELLDGLDpgvrviNVDSPAWADELAAHRDAEPPFRvaDPDDLFMLIFTS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 605 GSTGRPKGVMVGQTAIVNRLLWMQNHYPLTGEDVVAQKTPCSFDVSVWEFFWPFIA-GAKLVMaepeahRDPLAMQQFFA 683
Cdd:PRK07867 162 GTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVMAGWAVALAaGASIAL------RRKFSASGFLP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 684 ---EYGVTTTHFVPSMLAAFVAslTPQTARQSCATLKQVFcSGEALPADLcREWQQLTGAPLHNLYGPTEAAVDVSWYPA 760
Cdd:PRK07867 236 dvrRYGATYANYVGKPLSYVLA--TPERPDDADNPLRIVY-GNEGAPGDI-ARFARRFGCVVVDGFGSTEGGVAITRTPD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 761 FGEelaqvrGSsvpIGYPVwnTGLRILDA-MMHPVPPGVAGDLYLTGIQLAQGYLGRPDlTASRFIA---DPFAPGERM- 835
Cdd:PRK07867 312 TPP------GA---LGPLP--PGVAIVDPdTGTECPPAEDADGRLLNADEAIGELVNTA-GPGGFEGyynDPEADAERMr 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 836 ---YRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQAVTHAcVINQAAatgGDarQLVGYLVSQ 912
Cdd:PRK07867 380 ggvYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYA-VPDPVV---GD--QVMAALVLA 453
|
490
....*....|....*.
gi 16128569 913 SGLPLDTSALQAQLRE 928
Cdd:PRK07867 454 PGAKFDPDAFAEFLAA 469
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
481-888 |
1.10e-17 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 87.50 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 481 FSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTD 560
Cdd:cd05914 8 LTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVSD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 561 dqlprfsdvpnltslcynapltpqgsaplqlsqPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTGEDVV- 639
Cdd:cd05914 88 ---------------------------------EDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKIl 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 640 -----AQKTPCSFDvsvweFFWPFIAGAKLVMAEpeahRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPQTARQSCA 714
Cdd:cd05914 135 silplHHIYPLTFT-----LLLPLLNGAHVVFLD----KIPSAKIIALAFAQVTPTLGVPVPLVIEKIFKMDIIPKLTLK 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 715 TLKQ----------------------------VFCSGEA-LPADLCREWQQLtGAPLHNLYGPTEAAVDVSWYPAFGEEL 765
Cdd:cd05914 206 KFKFklakkinnrkirklafkkvheafggnikEFVIGGAkINPDVEEFLRTI-GFPYTIGYGMTETAPIISYSPPNRIRL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 766 AQVrgssvpiGYPVWNTGLRILDammhPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermYRTGDVARWL 845
Cdd:cd05914 285 GSA-------GKVIDGVEVRIDS----PDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW------FHTGDLGKID 347
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 16128569 846 DNGAVEYLGRSDDQLKI-RGQRIELGEIDRVMQALPDV---EQAVTH 888
Cdd:cd05914 348 AEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMPFVlesLVVVQE 394
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
465-853 |
1.13e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 87.82 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 465 AAKTPDAPA--LADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDD 542
Cdd:PRK13391 7 AQTTPDKPAviMASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 543 RLKMMLEDARPSLLITT-------------------------DDQLPRFSDVPNLTSLCYNAPLTpqgsaplqlSQPHHT 597
Cdd:PRK13391 87 EAAYIVDDSGARALITSaakldvarallkqcpgvrhrlvldgDGELEGFVGYAEAVAGLPATPIA---------DESLGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 598 AyIIFTSGSTGRPKGVM-------VGQTAIVNRLLWMQNHYpltGEDVV-------AQKTPCSFDVSVWEFfwpfiAGAK 663
Cdd:PRK13391 158 D-MLYSSGTTGRPKGIKrplpeqpPDTPLPLTAFLQRLWGF---RSDMVylspaplYHSAPQRAVMLVIRL-----GGTV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 664 LVMaepeAHRDPLAMQQFFAEYGVTTTHFVPSMlaaFVASLT-PQTARQS--CATLKQVFCSGEALPADLCREWQQLTGA 740
Cdd:PRK13391 229 IVM----EHFDAEQYLALIEEYGVTHTQLVPTM---FSRMLKlPEEVRDKydLSSLEVAIHAAAPCPPQVKEQMIDWWGP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 741 PLHNLYGPTEA----AVDvswypafGEELAQVRGSsvpIGYPVWNTgLRILDAMMHPVPPGVAGDLYL-TGIQLAqgYLG 815
Cdd:PRK13391 302 IIHEYYAATEGlgftACD-------SEEWLAHPGT---VGRAMFGD-LHILDDDGAELPPGEPGTIWFeGGRPFE--YLN 368
|
410 420 430
....*....|....*....|....*....|....*...
gi 16128569 816 RPDLTASRFIADPfapgeRMYRTGDVArWLDNGAVEYL 853
Cdd:PRK13391 369 DPAKTAEARHPDG-----TWSTVGDIG-YVDEDGYLYL 400
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
451-887 |
1.55e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 87.78 E-value: 1.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 451 EIPETT------LSALVAEQAAKTPDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHA 524
Cdd:PRK06710 14 EIPSTIsydiqpLHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 525 IVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTDDQLPRFSDVPNLT------------------SLCYNAPLTPQGS 586
Cdd:PRK06710 94 TLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLDLVFPRVTNVQSATkiehvivtriadflpfpkNLLYPFVQKKQSN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 587 APLQLSQPH------------------------HTAYIIFTSGSTGRPKGVMVGQTAIVNRLL----WMQNhyPLTGEDV 638
Cdd:PRK06710 174 LVVKVSESEtihlwnsvekevntgvevpcdpenDLALLQYTGGTTGFPKGVMLTHKNLVSNTLmgvqWLYN--CKEGEEV 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 639 VaqktpcsfdVSVWEFFWPFIAGAKLVMAEPEAHRDPLA----MQQFFAEYGVTTTHFVPSMLAAFVASL-TPQTARQSC 713
Cdd:PRK06710 252 V---------LGVLPFFHVYGMTAVMNLSIMQGYKMVLIpkfdMKMVFEAIKKHKVTLFPGAPTIYIALLnSPLLKEYDI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 714 ATLKQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAvDVSWYPAFGEElaQVRGSsvpIGYPVWNTGLRILDAMMHP 793
Cdd:PRK06710 323 SSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESS-PVTHSNFLWEK--RVPGS---IGVPWPDTEAMIMSLETGE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 794 V-PPGVAGDLYLTGIQLAQGYLGRPDLTASrFIADPFapgermYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEI 872
Cdd:PRK06710 397 AlPPGEIGEIVVKGPQIMKGYWNKPEETAA-VLQDGW------LHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREV 469
|
490
....*....|....*
gi 16128569 873 DRVMQALPDVEQAVT 887
Cdd:PRK06710 470 EEVLYEHEKVQEVVT 484
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
451-1044 |
2.90e-17 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 88.30 E-value: 2.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 451 EIPETTLSALvAEQAAKTPDAPAL------ADARYLFSYREMREQVVALANLLRERGVkPGDSVAVALPRSVFLTLALHA 524
Cdd:PRK05691 6 ELPLTLVQAL-QRRAAQTPDRLALrfladdPGEGVVLSYRDLDLRARTIAAALQARAS-FGDRAVLLFPSGPDYVAAFFG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 525 IVEAGAAWLPldtGYP--------DDRLKMMLEDARPSLLITTDDQLP--------RFSDVPNLtsLCYNA--PLTPQGS 586
Cdd:PRK05691 84 CLYAGVIAVP---AYPpesarrhhQERLLSIIADAEPRLLLTVADLRDsllqmeelAAANAPEL--LCVDTldPALAEAW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 587 APLQLsQPHHTAYIIFTSGSTGRPKGVMVGQTAIV-NRLLWMQNH-YPLTGEDVVAQKTPCSFDVS-VWEFFWPFIAGAK 663
Cdd:PRK05691 159 QEPAL-QPDDIAFLQYTSGSTALPKGVQVSHGNLVaNEQLIRHGFgIDLNPDDVIVSWLPLYHDMGlIGGLLQPIFSGVP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 664 LVMAEPEAHRD-PLAMQQFFAEYGVTTT---HFVPSMLAAFVASltPQTARQSCATLKQVFCSGEALPADLCREWQQ--- 736
Cdd:PRK05691 238 CVLMSPAYFLErPLRWLEAISEYGGTISggpDFAYRLCSERVSE--SALERLDLSRWRVAYSGSEPIRQDSLERFAEkfa 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 737 ---LTGAPLHNLYGPTEAAVDVSW------YPAF---GEELAQVR---GSSVPI---GYPVWNTGLRILD-AMMHPVPPG 797
Cdd:PRK05691 316 acgFDPDSFFASYGLAEATLFVSGgrrgqgIPALeldAEALARNRaepGTGSVLmscGRSQPGHAVLIVDpQSLEVLGDN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 798 VAGDLYLTGIQLAQGYLGRPDLTASRFIAdpfAPGERMYRTGDVArWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQ 877
Cdd:PRK05691 396 RVGEIWASGPSIAHGYWRNPEASAKTFVE---HDGRTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIEKTVE 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 878 A-LPDVEQAVTHACVINQAAATGGDARQLVGYLVSQSGLPldtSALQAQLRETLP------------------PHMVPVV 938
Cdd:PRK05691 472 ReVEVVRKGRVAAFAVNHQGEEGIGIAAEISRSVQKILPP---QALIKSIRQAVAeacqeapsvvlllnpgalPKTSSGK 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 939 LLQLPQLPLSANGKLDRKALpLPELKAQAPGRAPKAGSE--TIIAAAFSSLLGCDVQDADADFFALGGHSLLAMKLAAQL 1016
Cdd:PRK05691 549 LQRSACRLRLADGSLDSYAL-FPALQAVEAAQTAASGDElqARIAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVARL 627
|
650 660
....*....|....*....|....*...
gi 16128569 1017 SRQVARQVTPGQVMVASTVAKLATIIDA 1044
Cdd:PRK05691 628 RDELGIDLNLRQLFEAPTLAAFSAAVAR 655
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
462-933 |
3.07e-17 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 86.94 E-value: 3.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 462 AEQA---AKTPDAPALADA----RYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWL- 533
Cdd:cd05943 73 AENLlrhADADDPAAIYAAedgeRTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSs 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 534 --PlDTGYPD--DRLKMMledaRPSLLITTD---------DQLPRFSDV----PNLT---------------------SL 575
Cdd:cd05943 153 csP-DFGVPGvlDRFGQI----EPKVLFAVDaytyngkrhDVREKVAELvkglPSLLavvvvpytvaagqpdlskiakAL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 576 CYNAPLTPQGSAPLQLSQP--HHTAYIIFTSGSTGRPKGVMVGQTAIVnrllwMQN------HYPLTGEDVVAQKTPCSf 647
Cdd:cd05943 228 TLEDFLATGAAGELEFEPLpfDHPLYILYSSGTTGLPKCIVHGAGGTL-----LQHlkehilHCDLRPGDRLFYYTTCG- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 648 dvsvWeFFWPFIAGAKLVMAE------PEAHRDPLAMQQFFAEYGVTttHFVPSmlAAFV-----ASLTPQTARqSCATL 716
Cdd:cd05943 302 ----W-MMWNWLVSGLAVGATivlydgSPFYPDTNALWDLADEEGIT--VFGTS--AKYLdalekAGLKPAETH-DLSSL 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 717 KQVFCSGEALPAD----LCREWQqlTGAPLHNLYGPTE-------AAVDVSWYPafGEelAQVRGssvpIGYPVwntglR 785
Cdd:cd05943 372 RTILSTGSPLKPEsfdyVYDHIK--PDVLLASISGGTDiiscfvgGNPLLPVYR--GE--IQCRG----LGMAV-----E 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 786 ILDAMMHPVPpGVAGDLYLTGIQLAQ--GYLGRPDltASRFIADPFA--PGerMYRTGDVARWLDNGAVEYLGRSDDQLK 861
Cdd:cd05943 437 AFDEEGKPVW-GEKGELVCTKPFPSMpvGFWNDPD--GSRYRAAYFAkyPG--VWAHGDWIEITPRGGVVILGRSDGTLN 511
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128569 862 IRGQRIELGEIDRVMQALPDVEQAVthacVINQAAAtGGDARqLVGYLVSQSGLPLDTS---ALQAQLRETLPPH 933
Cdd:cd05943 512 PGGVRIGTAEIYRVVEKIPEVEDSL----VVGQEWK-DGDER-VILFVKLREGVELDDElrkRIRSTIRSALSPR 580
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
594-885 |
3.44e-17 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 84.64 E-value: 3.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 594 PHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTGEDVVAQKTPcsfdvsvweFFWPF------IA----GAK 663
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVP---------LFHCFgsvlgvLAclthGAT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 664 LVMaePEAHRDPLAMQQFFAEYGVTTTHFVPSMlaaFVASLT-PQTARQSCATLKQVFCSGEALPADLCREWQQLTGAP- 741
Cdd:cd05917 72 MVF--PSPSFDPLAVLEAIEKEKCTALHGVPTM---FIAELEhPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKd 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 742 LHNLYGPTEAAvDVSwYPAFGEELAQVRGSSVpiGYPVWNTGLRILDAMMHPVPP-GVAGDLYLTGIQLAQGYLGRPDLT 820
Cdd:cd05917 147 VTIAYGMTETS-PVS-TQTRTDDSIEKRVNTV--GRIMPHTEAKIVDPEGGIVPPvGVPGELCIRGYSVMKGYWNDPEKT 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128569 821 ASRfiadpfAPGERMYRTGDVARWLDNGAVEYLGRSDDQLkIRG-QRIELGEIDRVMQALPDVEQA 885
Cdd:cd05917 223 AEA------IDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGgENIYPREIEEFLHTHPKVSDV 281
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
475-892 |
5.06e-17 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 86.10 E-value: 5.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 475 ADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPS 554
Cdd:PRK04319 68 ASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAK 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 555 LLITTDDQLPR--FSDVPNL-TSLCYNAPLTPQG--------------SAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQ 617
Cdd:PRK04319 148 VLITTPALLERkpADDLPSLkHVLLVGEDVEEGPgtldfnalmeqasdEFDIEWTDREDGAILHYTSGSTGKPKGVLHVH 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 618 TAivnrllwMQNHYpLTGEDVVAQKTP----CSFD---V--SVWEFFWPFIAGAKLVMAEPEAhrDPLAMQQFFAEYGVT 688
Cdd:PRK04319 228 NA-------MLQHY-QTGKYVLDLHEDdvywCTADpgwVtgTSYGIFAPWLNGATNVIDGGRF--SPERWYRILEDYKVT 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 689 TTHFVPS---MLaafvASLTPQTARQSC-ATLKQVFCSGEALPADLCREWQQLTGAPLHNLYGPTE-AAVDVSWYPAFge 763
Cdd:PRK04319 298 VWYTAPTairML----MGAGDDLVKKYDlSSLRHILSVGEPLNPEVVRWGMKVFGLPIHDNWWMTEtGGIMIANYPAM-- 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 764 elaQVR-GSsvpIGYPVWNTGLRILDAMMHPVPPGVAGDLYL-TGI-QLAQGYLGRPDLTASRFIADpfapgerMYRTGD 840
Cdd:PRK04319 372 ---DIKpGS---MGKPLPGIEAAIVDDQGNELPPNRMGNLAIkKGWpSMMRGIWNNPEKYESYFAGD-------WYVSGD 438
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 16128569 841 VARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMqalpdVE-QAVTHACVI 892
Cdd:PRK04319 439 SAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKL-----MEhPAVAEAGVI 486
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
453-886 |
1.73e-16 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 83.89 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 453 PETTLSALvaEQAAKT-PDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAA 531
Cdd:cd12118 3 PLTPLSFL--ERAAAVyPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 532 WLPLDTGYPDDRLKMMLEDARPSLLITTddqlprfsdvpnlTSLCYNAPLTPQ-GSAPLQLSQPHHTAYII-FTSGSTGR 609
Cdd:cd12118 81 LNALNTRLDAEEIAFILRHSEAKVLFVD-------------REFEYEDLLAEGdPDFEWIPPADEWDPIALnYTSGTTGR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 610 PKGVMVGQ-----TAIVNRLLWMQNHYPltgedvVAQKTPCSFDVSVWEFFW--PFIAGAKLVMaepeAHRDPLAMQQFF 682
Cdd:cd12118 148 PKGVVYHHrgaylNALANILEWEMKQHP------VYLWTLPMFHCNGWCFPWtvAAVGGTNVCL----RKVDAKAIYDLI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 683 AEYGVttTHF-----VPSMLAAfvaslTPQTARQSCATLKQVFCSGEALPADLCREWQQLTGAPLHnLYGPTEA---AVD 754
Cdd:cd12118 218 EKHKV--THFcgaptVLNMLAN-----APPSDARPLPHRVHVMTAGAPPPAAVLAKMEELGFDVTH-VYGLTETygpATV 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 755 VSWYPAF----GEELAQVRGSSvPIGYPVwNTGLRILDA-MMHPVP-PGV-AGDLYLTGIQLAQGYLGRPDLTasrfiAD 827
Cdd:cd12118 290 CAWKPEWdelpTEERARLKARQ-GVRYVG-LEEVDVLDPeTMKPVPrDGKtIGEIVFRGNIVMKGYLKNPEAT-----AE 362
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 828 PFAPGerMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDV-EQAV 886
Cdd:cd12118 363 AFRGG--WFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVlEAAV 420
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
451-886 |
1.92e-16 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 84.30 E-value: 1.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 451 EIPET---TLSALVAEQAAKTPDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVE 527
Cdd:PRK07059 16 EIDASqypSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 528 AGAAWLPLDTGYPDDRLKMMLEDARPSLLI------TTDDQLPRFSDVPNLT---------------------------- 573
Cdd:PRK07059 96 AGYVVVNVNPLYTPRELEHQLKDSGAEAIVvlenfaTTVQQVLAKTAVKHVVvasmgdllgfkghivnfvvrrvkkmvpa 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 574 -----SLCYNAPLTP---QGSAPLQLsQPHHTAYIIFTSGSTGRPKGVMVGQTAIV-NRL---LWMQNHYpLTGEDVVAQ 641
Cdd:PRK07059 176 wslpgHVRFNDALAEgarQTFKPVKL-GPDDVAFLQYTGGTTGVSKGATLLHRNIVaNVLqmeAWLQPAF-EKKPRPDQL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 642 KTPCS------FDVSVWEFFWPFIAGAKLVMAEPeahRDplaMQQFFAEYGVTTTHFVPSMLAAFVASL-TPQTARQSCA 714
Cdd:PRK07059 254 NFVCAlplyhiFALTVCGLLGMRTGGRNILIPNP---RD---IPGFIKELKKYQVHIFPAVNTLYNALLnNPDFDKLDFS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 715 TLKQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVDVSWYPAFGEELAqvrGSsvpIGYPVWNTGLRILDAMMHPV 794
Cdd:PRK07059 328 KLIVANGGGMAVQRPVAERWLEMTGCPITEGYGLSETSPVATCNPVDATEFS---GT---IGLPLPSTEVSIRDDDGNDL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 795 PPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDR 874
Cdd:PRK07059 402 PLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGF------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEE 475
|
490
....*....|...
gi 16128569 875 VMQALPDV-EQAV 886
Cdd:PRK07059 476 VVASHPGVlEVAA 488
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
484-886 |
4.66e-16 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 82.92 E-value: 4.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 484 REMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLIT----- 558
Cdd:PLN02860 36 HEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVTdetcs 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 559 ------TDDQLPRF-----------SDVPNLTSLCYNAPLTPQGSAPLQL---SQPHHTAYIIFTSGSTGRPKGVMVGQT 618
Cdd:PLN02860 116 swyeelQNDRLPSLmwqvflespssSVFIFLNSFLTTEMLKQRALGTTELdyaWAPDDAVLICFTSGTTGRPKGVTISHS 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 619 AIVNRLLWMQNHYPLTGEDVVAQKTP-CSfdvsvweffwpfIAGAKLVMAEPEAHRDPLAMQQFFA--------EYGVTT 689
Cdd:PLN02860 196 ALIVQSLAKIAIVGYGEDDVYLHTAPlCH------------IGGLSSALAMLMVGACHVLLPKFDAkaalqaikQHNVTS 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 690 THFVPSMLAAFVASLTPQTARQSCATLKQVFCSGEALPADLCREWQQL-TGAPLHNLYGPTEAAVDVSWYP--------- 759
Cdd:PLN02860 264 MITVPAMMADLISLTRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLfPNAKLFSAYGMTEACSSLTFMTlhdptlesp 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 760 -AFGEELAQVRGSSVP------IGYPVWNTGLRI-LDAMMHpvppgvAGDLYLTGIQLAQGYLGRPDLTASRFIADPFap 831
Cdd:PLN02860 344 kQTLQTVNQTKSSSVHqpqgvcVGKPAPHVELKIgLDESSR------VGRILTRGPHVMLGYWGQNSETASVLSNDGW-- 415
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 16128569 832 germYRTGDVArWLDN-GAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQAV 886
Cdd:PLN02860 416 ----LDTGDIG-WIDKaGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVV 466
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
5-424 |
5.26e-16 |
|
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380459 [Multi-domain] Cd Length: 419 Bit Score: 82.11 E-value: 5.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 5 LPLVAAQPGIWMAEKLSELPSAWSVAHYVELTGEVDSPLLARAVVAGLAQADTLRMRFTEDN-GEVWQWVDDALTFELPE 83
Cdd:cd19536 2 YPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGlGQPVQVVHRQAQVPVTE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 84 IiDLRTNIDPHGTAQALMQADLQQDLRVDSGKPLVFHQLIQVADNRWYWYQRYHHLLVDGFSFPAITRQIANIYCTWLRG 163
Cdd:cd19536 82 L-DLTPLEEQLDPLRAYKEETKIRRFDLGRAPLVRAALVRKDERERFLLVISDHHSILDGWSLYLLVKEILAVYNQLLEY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 164 EPTPASPFTPFADVVeeyQQYRESEAWQRDAAFWAEQRRQLPPPASLSPAPLPGRSASADILRLKLEFTDGEFRQLATQl 243
Cdd:cd19536 161 KPLSLPPAQPYRDFV---AHERASIQQAASERYWREYLAGATLATLPALSEAVGGGPEQDSELLVSVPLPVRSRSLAKR- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 244 SGVQRTDLALALAALWLGRLCNRMDYAAGFIFMRRL--GSAALTATGPVLNVLPLGIHiAAQETLPELATRLAAQLKKMR 321
Cdd:cd19536 237 SGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSeeTTGAERLLGLFLNTLPLRVT-LSEETVEDLLKRAQEQELESL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 322 RHQRYDaeqiVRDSGRAAGDEPLFGPVLNIKVFDYQLDIP----DVQAQTHTLATGPVNDLELALFPDVHGD-LSIEILA 396
Cdd:cd19536 316 SHEQVP----LADIQRCSEGEPLFDSIVNFRHFDLDFGLPewgsDEGMRRGLLFSEFKSNYDVNLSVLPKQDrLELKLAY 391
|
410 420
....*....|....*....|....*...
gi 16128569 397 NKQRYDEPTLIQHAERLKMLIAQFAADP 424
Cdd:cd19536 392 NSQVLDEEQAQRLAAYYKSAIAELATAP 419
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
465-885 |
1.02e-15 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 81.46 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 465 AAKTPDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRL 544
Cdd:PRK09029 13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 545 KMMLedarPSLLITTDDQLPRFSDVPNLTSLCYNAPLTPQGSAPlqlsQPHHTAYIIFTSGSTGRPKgvmvgqtAIVNRL 624
Cdd:PRK09029 93 EELL----PSLTLDFALVLEGENTFSALTSLHLQLVEGAHAVAW----QPQRLATMTLTSGSTGLPK-------AAVHTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 625 lwmQNHypLTGEDVVAQKTPCS-----------FDVS----VWEffWPFiAGAKLVMAEPEAHRDPLAmqqffaeyGVTT 689
Cdd:PRK09029 158 ---QAH--LASAEGVLSLMPFTaqdswllslplFHVSgqgiVWR--WLY-AGATLVVRDKQPLEQALA--------GCTH 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 690 THFVPSMLAAFVASLTPQTarqscaTLKQVFCSGEALPADLCREWQQL-----TGaplhnlYGPTEAAVDVSWYPAfgEE 764
Cdd:PRK09029 222 ASLVPTQLWRLLDNRSEPL------SLKAVLLGGAAIPVELTEQAEQQgircwCG------YGLTEMASTVCAKRA--DG 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 765 LAQVrgssvpiGYPVWNTGLRIldammhpvppgVAGDLYLTGIQLAQGYLGRPDLTasrfiadPFAPGERMYRTGDVARW 844
Cdd:PRK09029 288 LAGV-------GSPLPGREVKL-----------VDGEIWLRGASLALGYWRQGQLV-------PLVNDEGWFATRDRGEW 342
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 16128569 845 lDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQA 885
Cdd:PRK09029 343 -QNGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQV 382
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
482-932 |
1.15e-15 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 81.25 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 482 SYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAwlpldtgypddrlkmmledarPSLLittdd 561
Cdd:cd05940 5 TYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAV---------------------AALI----- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 562 qlprfsdvpnltslcyNAPLTPQGSA-PLQLSQPHH----TAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTGE 636
Cdd:cd05940 59 ----------------NYNLRGESLAhCLNVSSAKHlvvdAALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPS 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 637 DVVAQKTPCSFDV-SVWEFFWPFIAGAKLVMaepeahRDPLAMQQFFAE---YGVTTTHFVPSMLAAFVAslTPQTARQS 712
Cdd:cd05940 123 DVLYTCLPLYHSTaLIVGWSACLASGATLVI------RKKFSASNFWDDirkYQATIFQYIGELCRYLLN--QPPKPTER 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 713 CATLKQVFcsGEALPADLCREWQQLTGAP-LHNLYGPTEAavDVSWYPAFGEELAQVR-GSSVPIGYPV------WNTG- 783
Cdd:cd05940 195 KHKVRMIF--GNGLRPDIWEEFKERFGVPrIAEFYAATEG--NSGFINFFGKPGAIGRnPSLLRKVAPLalvkydLESGe 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 784 -LRILDAMMHPVPPGVAGDL--YLTGIQLAQGYLGrPDLTASRFIADPFAPGERMYRTGDVARWLDNGAVEYLGRSDDQL 860
Cdd:cd05940 271 pIRDAEGRCIKVPRGEPGLLisRINPLEPFDGYTD-PAATEKKILRDVFKKGDAWFNTGDLMRLDGEGFWYFVDRLGDTF 349
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128569 861 KIRGQRIELGEIDRVMQALPDVEQAVTHACVInqaaaTGGDARQLVGYLVSQSGLPLDTSALQAQLRETLPP 932
Cdd:cd05940 350 RWKGENVSTTEVAAVLGAFPGVEEANVYGVQV-----PGTDGRAGMAAIVLQPNEEFDLSALAAHLEKNLPG 416
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
453-933 |
1.71e-15 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 81.46 E-value: 1.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 453 PETTLSALVAEQAAKTPDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALP-RSVFLTLALhAIVEAGAA 531
Cdd:PRK08279 35 SKRSLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMEnRPEYLAAWL-GLAKLGAV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 532 WLPLDTGYPDDRLKMMLEDARPSLLITTDDQLPRFSDVPNLTSL----------CYNAPLTPQGSAPLQLSQPHH----- 596
Cdd:PRK08279 114 VALLNTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLARpprlwvaggdTLDDPEGYEDLAAAAAGAPTTnpasr 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 597 -------TAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTGEDVVAQKTPCSFD---VSVWeffwpfiaGAKLVM 666
Cdd:PRK08279 194 sgvtakdTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYHNtggTVAW--------SSVLAA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 667 AEPEAHRDPLAMQQFFAE---YGVTTTHFVPSMLAAFVASltPQTARQSCATLKQVFcsGEALPADLCREWQQLTGAP-L 742
Cdd:PRK08279 266 GATLALRRKFSASRFWDDvrrYRATAFQYIGELCRYLLNQ--PPKPTDRDHRLRLMI--GNGLRPDIWDEFQQRFGIPrI 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 743 HNLYGPTEAavDVSWYPAFGeelaqVRGSsvpIGY-PVWN------------TG--LRILDAMMHPVPPGVAGDLyLTGI 807
Cdd:PRK08279 342 LEFYAASEG--NVGFINVFN-----FDGT---VGRvPLWLahpyaivkydvdTGepVRDADGRCIKVKPGEVGLL-IGRI 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 808 QLAQ---GYlGRPDLTASRFIADPFAPGERMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQ 884
Cdd:PRK08279 411 TDRGpfdGY-TDPEASEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEE 489
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 16128569 885 AVTHACVInqaAATGGDArqlvGY--LVSQSGLPLDTSALQAQLRETLPPH 933
Cdd:PRK08279 490 AVVYGVEV---PGTDGRA----GMaaIVLADGAEFDLAALAAHLYERLPAY 533
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
463-886 |
5.68e-15 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 79.71 E-value: 5.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 463 EQA-AKTPDAPALADARYLFSYREMREQVVALANLLR-ERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYP 540
Cdd:PRK08974 30 EQAvARYADQPAFINMGEVMTFRKLEERSRAFAAYLQnGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 541 DDRLKMMLEDARPS------------------------LLITTDDQLPRfsdvPNLT----SLCYNAPLTPQGSAP---- 588
Cdd:PRK08974 110 PRELEHQLNDSGAKaivivsnfahtlekvvfktpvkhvILTRMGDQLST----AKGTlvnfVVKYIKRLVPKYHLPdais 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 589 ----------LQLSQPH----HTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHY-PL--TGEDVVAQKTPCS--FDV 649
Cdd:PRK08974 186 frsalhkgrrMQYVKPElvpeDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYgPLlhPGKELVVTALPLYhiFAL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 650 SVWEFFWPFIAGAKLVMAEPeahRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASltPQTARQSCATLKQVFCSGEALPAD 729
Cdd:PRK08974 266 TVNCLLFIELGGQNLLITNP---RDIPGFVKELKKYPFTAITGVNTLFNALLNN--EEFQELDFSSLKLSVGGGMAVQQA 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 730 LCREWQQLTGAPLHNLYGPTEAAVDVSWYPAfgeELAQVRGSsvpIGYPVWNTGLRILDAMMHPVPPGVAGDLYLTGIQL 809
Cdd:PRK08974 341 VAERWVKLTGQYLLEGYGLTECSPLVSVNPY---DLDYYSGS---IGLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQV 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128569 810 AQGYLGRPDLTASrFIADPFapgermYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQAV 886
Cdd:PRK08974 415 MLGYWQRPEATDE-VIKDGW------LATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVA 484
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
459-930 |
1.74e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 78.27 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 459 ALVAEQAAKTPDAPALADARYLFSYREMREQVVALANLLR-ERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWL---P 534
Cdd:PRK05677 28 AVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQqHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVntnP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 535 LDTG------YPDDRLKMML---------EDARPSL----LITTD--DQLPRFSD-------------VPNLT---SLCY 577
Cdd:PRK05677 108 LYTAremehqFNDSGAKALVclanmahlaEKVLPKTgvkhVIVTEvaDMLPPLKRllinavvkhvkkmVPAYHlpqAVKF 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 578 NAPLTPQGSAPLQLSQPH--HTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQnhyPLT------GEDVVAQKTPC---- 645
Cdd:PRK05677 188 NDALAKGAGQPVTEANPQadDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCR---ALMgsnlneGCEILIAPLPLyhiy 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 646 SFDVSVweFFWPFIAGAKLVMAEPeahRDPLAMQQFFAEYGVTTthFVpSMLAAFVASLTPQTARQ-SCATLKQVFCSGE 724
Cdd:PRK05677 265 AFTFHC--MAMMLIGNHNILISNP---RDLPAMVKELGKWKFSG--FV-GLNTLFVALCNNEAFRKlDFSALKLTLSGGM 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 725 ALPADLCREWQQLTGAPLHNLYGPTEAAVDVSWYPAFGEELAQvrgssvpIGYPVWNTGLRILDAMMHPVPPGVAGDLYL 804
Cdd:PRK05677 337 ALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGT-------IGIPVPSTLCKVIDDDGNELPLGEVGELCV 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 805 TGIQLAQGYLGRPDLTASRFIADPFapgermYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQ 884
Cdd:PRK05677 410 KGPQVMKGYWQRPEATDEILDSDGW------LKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQ 483
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 16128569 885 AVThacvINQAAATGGDARQLvgYLVSQSGLPLDTSALQAQLRETL 930
Cdd:PRK05677 484 CAA----IGVPDEKSGEAIKV--FVVVKPGETLTKEQVMEHMRANL 523
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
5-424 |
3.14e-14 |
|
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380464 [Multi-domain] Cd Length: 401 Bit Score: 76.19 E-value: 3.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 5 LPLVAAQPGIwMAEKLSELPSAWSVaHYVELTGEVDSPLLARAVVAGLAQADTLRMRFTEDNGE--VWQWVDDALTfelP 82
Cdd:cd19542 2 YPCTPMQEGM-LLSQLRSPGLYFNH-FVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSAEgtFLQVVLKSLD---P 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 83 EIIDLRTNIDphgTAQALMQADLQQdlRVDSGKPLVFHQLIQVADNRWYWYQRYHHLLVDGFSFPAITRQIANIYctwlR 162
Cdd:cd19542 77 PIEEVETDED---SLDALTRDLLDD--PTLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAY----N 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 163 GEPTPasPFTPFADvveeYQQYRESEAWQRDAAFWAEQ---RRQLPPPASLSPAPLPGRSASADILRLKLEftdgEFRQ- 238
Cdd:cd19542 148 GQLLP--PAPPFSD----YISYLQSQSQEESLQYWRKYlqgASPCAFPSLSPKRPAERSLSSTRRSLAKLE----AFCAs 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 239 -LATQLSGVQrtdlalalaALW---LGRLCNRMDYAAGFIFMRRLGS--AALTATGPVLNVLPLGIHIAAQETLPELATR 312
Cdd:cd19542 218 lGVTLASLFQ---------AAWalvLARYTGSRDVVFGYVVSGRDLPvpGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQ 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 313 LAAQLKKMRRHQRYDAEQIVRDSGRaAGDEPLFGPVLNIKVFDYQLDIPDV-QAQTHTLATGPVNDLELALFPDVHGD-L 390
Cdd:cd19542 289 LQQQYLRSLPHQHLSLREIQRALGL-WPSGTLFNTLVSYQNFEASPESELSgSSVFELSAAEDPTEYPVAVEVEPSGDsL 367
|
410 420 430
....*....|....*....|....*....|....
gi 16128569 391 SIEILANKQRYDEPTLIQHAERLKMLIAQFAADP 424
Cdd:cd19542 368 KVSLAYSTSVLSEEQAEELLEQFDDILEALLANP 401
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
463-882 |
3.18e-14 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 77.25 E-value: 3.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 463 EQAAKTPDAPALA---------DARY-LFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAW 532
Cdd:PRK09274 14 RAAQERPDQLAVAvpggrgadgKLAYdELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 533 LPLDTGYPDDRLKMMLEDARPSLLIT-TDDQLPR------FSDV-PNLT---SLCYNAP-------LTPQGSAPLQLSQP 594
Cdd:PRK09274 94 VLVDPGMGIKNLKQCLAEAQPDAFIGiPKAHLARrlfgwgKPSVrRLVTvggRLLWGGTtlatllrDGAAAPFPMADLAP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 595 HHTAYIIFTSGSTGRPKGV------MVGQ-TAIvnrllwmQNHYPLtgedvvaqkTPCSFDVSVWEFFWPFiaGAKLVMA 667
Cdd:PRK09274 174 DDMAAILFTSGSTGTPKGVvythgmFEAQiEAL-------REDYGI---------EPGEIDLPTFPLFALF--GPALGMT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 668 E--PE------AHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLtpQTARQSCATLKQVFCSGEALPADLcreWQQLT- 738
Cdd:PRK09274 236 SviPDmdptrpATVDPAKLFAAIERYGVTNLFGSPALLERLGRYG--EANGIKLPSLRRVISAGAPVPIAV---IERFRa 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 739 ----GAPLHNLYGPTEaAVDVSwypAFG-----EELAQV--RGSSVPIGYPVWNTGLRILDAMMHP---------VPPGV 798
Cdd:PRK09274 311 mlppDAEILTPYGATE-ALPIS---SIEsreilFATRAAtdNGAGICVGRPVDGVEVRIIAISDAPipewddalrLATGE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 799 AGDLYLTGIQLAQGYLGRPDLTASRFIADPfaPGERMYRTGDVArWLDN-GAVEYLGRSDDQLKIRGQRIELGEIDRVMQ 877
Cdd:PRK09274 387 IGEIVVAGPMVTRSYYNRPEATRLAKIPDG--QGDVWHRMGDLG-YLDAqGRLWFCGRKAHRVETAGGTLYTIPCERIFN 463
|
....*
gi 16128569 878 ALPDV 882
Cdd:PRK09274 464 THPGV 468
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
465-958 |
3.72e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 76.74 E-value: 3.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 465 AAKTPDAPALADARYLFSYREMREQVVALANLLRERGVKPgDSVAVALPRSV-FLTLALHAiveAGAAW--LPLDTGYPD 541
Cdd:PRK07638 11 ASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKN-KTIAILLENRIeFLQLFAGA---AMAGWtcVPLDIKWKQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 542 DRLKMMLEDARPSLLITTDDQLPRFSDV--PNLTSLCYNAPLTPQGSAPLQLSQPHHTA-YIIFTSGSTGRPKGVMVGQT 618
Cdd:PRK07638 87 DELKERLAISNADMIVTERYKLNDLPDEegRVIEIDEWKRMIEKYLPTYAPIENVQNAPfYMGFTSGSTGKPKAFLRAQQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 619 AivnrllWMQNHYPlTGEDVVAQKT-----PCSFDVSVweFFWP-----FIAGAKLVMAE--PEAHRDPLAMQQFFAEYG 686
Cdd:PRK07638 167 S------WLHSFDC-NVHDFHMKREdsvliAGTLVHSL--FLYGaistlYVGQTVHLMRKfiPNQVLDKLETENISVMYT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 687 vttthfVPSMLAAFV-ASLTPQTarqscaTLKqVFCSGEALPADLCREWQ-QLTGAPLHNLYGPTEaavdVSWYPAFGEE 764
Cdd:PRK07638 238 ------VPTMLESLYkENRVIEN------KMK-IISSGAKWEAEAKEKIKnIFPYAKLYEFYGASE----LSFVTALVDE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 765 LAQVRGSSVpiGYPVWNTGLRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGrpdltASRFIADPFAPGermYRTGDVARW 844
Cdd:PRK07638 301 ESERRPNSV--GRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYII-----GGVLARELNADG---WMTVRDVGY 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 845 LDNGAVEYL-GRSDDQLKIRGQRIELGEIDRVMQALPDVEQAVthacVINQAAATGGDarQLVGYLVSQSglplDTSALQ 923
Cdd:PRK07638 371 EDEEGFIYIvGREKNMILFGGINIFPEEIESVLHEHPAVDEIV----VIGVPDSYWGE--KPVAIIKGSA----TKQQLK 440
|
490 500 510
....*....|....*....|....*....|....*
gi 16128569 924 AQLRETLPPHMVPVVLLQLPQLPLSANGKLDRKAL 958
Cdd:PRK07638 441 SFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEA 475
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
770-1045 |
9.99e-14 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 73.25 E-value: 9.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 770 GSSVPIGYPVWNTGLRILDAMMHPVPPGVAGDLYLTGIQLAQGYLG---RPDLTASRFIADPFAPGERMYRTGDVARWLD 846
Cdd:COG3433 10 PPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLlriRLLAAAARAPFIPVPYPAQPGRQADDLRLLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 847 NGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVeqavtHACVINQAAATGGDARQLVGYLVSQSGLPLDTSALQAQL 926
Cdd:COG3433 90 RRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAA-----AVVRVAVLAALRGAGVGLLLIVGAVAALDGLAAAAALAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 927 RETLPPHMVPVVLLQLPQLPLSANGKLDRKALPLPELKAQAPGRAPKAG------SETIIAAAFSSLLGCDVQ--DADAD 998
Cdd:COG3433 165 LDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASPAPaletalTEEELRADVAELLGVDPEeiDPDDN 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 16128569 999 FFALGGHSLLAMKLAAQLsRQVARQVTPGQVMVASTVAKLATIIDAE 1045
Cdd:COG3433 245 LFDLGLDSIRLMQLVERW-RKAGLDVSFADLAEHPTLAAWWALLAAA 290
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
599-930 |
1.28e-13 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 73.59 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 599 YIIFTSGSTGRPKGVMVGQTAivnrllWM-----QNH-YPLTGEDVVAQKTPCSFDVSVWEFFWPFIAGAKLVMaepEAH 672
Cdd:cd17633 4 YIGFTSGTTGLPKAYYRSERS------WIesfvcNEDlFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIG---QRK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 673 RDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPqtarqsCATLKQVFCSGEALPADLCREWQQltGAPLHNL---YGPT 749
Cdd:cd17633 75 FNPKSWIRKINQYNATVIYLVPTMLQALARTLEP------ESKIKSIFSSGQKLFESTKKKLKN--IFPKANLiefYGTS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 750 EAAVdVSWypAFGEELAQvRGSsvpIGYPVWNTGLRILDAmmhpvPPGVAGDLYLTGIQLAQGYLGRPDLTASRFiadpf 829
Cdd:cd17633 147 ELSF-ITY--NFNQESRP-PNS---VGRPFPNVEIEIRNA-----DGGEIGKIFVKSEMVFSGYVRGGFSNPDGW----- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 830 apgermYRTGDVArWLDNGAVEYL-GRSDDQLKIRGQRIELGEIDRVMQALPDVEQAVthacVINQAAATGGdarQLVGY 908
Cdd:cd17633 210 ------MSVGDIG-YVDEEGYLYLvGRESDMIIIGGINIFPTEIESVLKAIPGIEEAI----VVGIPDARFG---EIAVA 275
|
330 340
....*....|....*....|..
gi 16128569 909 LVsqSGLPLDTSALQAQLRETL 930
Cdd:cd17633 276 LY--SGDKLTYKQLKRFLKQKL 295
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
464-886 |
1.61e-13 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 75.29 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 464 QAAKTPDAPAL------ADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDT 537
Cdd:cd05966 62 HLKERGDKVAIiwegdePDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 538 GYPDDRLKMMLEDARPSLLITTDDQLPRFSDVPnLTSLCYNA--------------------PLTPQ------------- 584
Cdd:cd05966 142 GFSAESLADRINDAQCKLVITADGGYRGGKVIP-LKEIVDEAlekcpsvekvlvvkrtggevPMTEGrdlwwhdlmakqs 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 585 GSAPLQLSQPHHTAYIIFTSGSTGRPKGVmVGQTAivNRLLW----MQNHYPLTGEDVVAqktpCSFDVSvweffW---- 656
Cdd:cd05966 221 PECEPEWMDSEDPLFILYTSGSTGKPKGV-VHTTG--GYLLYaattFKYVFDYHPDDIYW----CTADIG-----Witgh 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 657 ------PFIAGAKLVMAE-----PEAHRdplaMQQFFAEYGVTTTHFVPS---MLAAFVASLTPQTARQSCATLKQVfcs 722
Cdd:cd05966 289 syivygPLANGATTVMFEgtptyPDPGR----YWDIVEKHKVTIFYTAPTairALMKFGDEWVKKHDLSSLRVLGSV--- 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 723 GEALPAD--------LCRE--------WQQLTG----APLHNLYG--PTEAAvdvswYPAFGEELAqvrgssvpigypvw 780
Cdd:cd05966 362 GEPINPEawmwyyevIGKErcpivdtwWQTETGgimiTPLPGATPlkPGSAT-----RPFFGIEPA-------------- 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 781 ntglrILDAMMHPVPPGVAGDLYLT----GIqlAQGYLGRPDltasRFIADPFAPGERMYRTGDVARWLDNGAVEYLGRS 856
Cdd:cd05966 423 -----ILDEEGNEVEGEVEGYLVIKrpwpGM--ARTIYGDHE----RYEDTYFSKFPGYYFTGDGARRDEDGYYWITGRV 491
|
490 500 510
....*....|....*....|....*....|.
gi 16128569 857 DDQLKIRGQRIELGEIDRVMQALPDV-EQAV 886
Cdd:cd05966 492 DDVINVSGHRLGTAEVESALVAHPAVaEAAV 522
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
450-875 |
5.22e-13 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 73.09 E-value: 5.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 450 VEIPE-TTLSALVAEQAAKTPDAPALADAR--YLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIV 526
Cdd:PLN02246 17 IYIPNhLPLHDYCFERLSEFSDRPCLIDGAtgRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGAS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 527 EAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTD---DQLPRFSDVPNLTSLCYNAP----------LTPQGSAPLQLS- 592
Cdd:PLN02246 97 RRGAVTTTANPFYTPAEIAKQAKASGAKLIITQScyvDKLKGLAEDDGVTVVTIDDPpegclhfselTQADENELPEVEi 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 593 QPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLlwMQ-------NHYpLTGEDVVAQKTP------------CSFDVsvwe 653
Cdd:PLN02246 177 SPDDVVALPYSSGTTGLPKGVMLTHKGLVTSV--AQqvdgenpNLY-FHSDDVILCVLPmfhiyslnsvllCGLRV---- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 654 ffwpfiAGAKLVMAEPEAhrdpLAMQQFFAEYGVTTTHFVPSMLAAFVASltPQTARQSCATLKQVFcSGEAlPadLCRE 733
Cdd:PLN02246 250 ------GAAILIMPKFEI----GALLELIQRHKVTIAPFVPPIVLAIAKS--PVVEKYDLSSIRMVL-SGAA-P--LGKE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 734 WQQLTGAPLHNL-----YGPTEAAVDVSWYPAFGEELAQVRGSSVpiGYPVWNTGLRILDammhP-----VPPGVAGDLY 803
Cdd:PLN02246 314 LEDAFRAKLPNAvlgqgYGMTEAGPVLAMCLAFAKEPFPVKSGSC--GTVVRNAELKIVD----PetgasLPRNQPGEIC 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128569 804 LTGIQLAQGYLGRPDLTAsrfiadpfapgermyRTGDVARWLDNGAVEYLGRsDDQLKIrgqrielgeIDRV 875
Cdd:PLN02246 388 IRGPQIMKGYLNDPEATA---------------NTIDKDGWLHTGDIGYIDD-DDELFI---------VDRL 434
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
483-624 |
5.49e-13 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 73.50 E-value: 5.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 483 YREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAG--AAWLPLDTGYPD-----DRLKMMLEDARPSL 555
Cdd:PRK09192 52 YQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGlvPVPLPLPMGFGGresyiAQLRGMLASAQPAA 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128569 556 LITTDDQLPRFSDVPNLTSLCYNAPLT-----PQGSAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRL 624
Cdd:PRK09192 132 IITPDELLPWVNEATHGNPLLHVLSHAwfkalPEADVALPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANL 205
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
4-200 |
6.50e-13 |
|
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380454 [Multi-domain] Cd Length: 427 Bit Score: 72.39 E-value: 6.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 4 HLPLVAAQPGIWMAEKLSELPSAWSVAHYVELTGEVDSPLLARAVVAGLAQADTLRMRFTEDNGEVWQWVDDALTFELPe 83
Cdd:cd19531 1 PLPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQVILPPLPLPLP- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 84 IIDLRT--NIDPHGTAQALMQADLQQ--DLRVDsgkPLVFHQLIQVADNRWYWYQRYHHLLVDGFSFPAITRQIANIYCT 159
Cdd:cd19531 80 VVDLSGlpEAEREAEAQRLAREEARRpfDLARG---PLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16128569 160 WLRGEPtpaSPFTP----FADVVEEYQQYRESEAWQRDAAFWAEQ 200
Cdd:cd19531 157 FLAGRP---SPLPPlpiqYADYAVWQREWLQGEVLERQLAYWREQ 198
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
461-882 |
7.28e-13 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 72.93 E-value: 7.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 461 VAEQAAKT-PDAPALADARYLFSYREMREQVVALANLLRER-GVKPGDSVAVALPRSVFLTLALHAIVEAGAAWL---PL 535
Cdd:PRK12492 29 VFERSCKKfADRPAFSNLGVTLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVntnPL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 536 -----------DTG-----------------YPDDRLKMMLE----DARPSL---LITT-----DDQLPRFSdVPNLTSL 575
Cdd:PRK12492 109 ytaremrhqfkDSGaralvylnmfgklvqevLPDTGIEYLIEakmgDLLPAAkgwLVNTvvdkvKKMVPAYH-LPQAVPF 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 576 cYNAPLTPQGSAPLQLSQPHH-TAYIIFTSGSTGRPKGVMVGQTAIVNRLLW----MQNHYP------LTGEDVVAQKTP 644
Cdd:PRK12492 188 -KQALRQGRGLSLKPVPVGLDdIAVLQYTGGTTGLAKGAMLTHGNLVANMLQvracLSQLGPdgqplmKEGQEVMIAPLP 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 645 CSFdvsvwefFWPFIAGAKLVMAEPEAH------RD------PLAMQQFFAEYGVTTThfvpsmlaaFVASLT-PQTARQ 711
Cdd:PRK12492 267 LYH-------IYAFTANCMCMMVSGNHNvlitnpRDipgfikELGKWRFSALLGLNTL---------FVALMDhPGFKDL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 712 SCATLKQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVDVSWYPaFGEelaQVRGSSVpiGYPVWNTGLRILDAMM 791
Cdd:PRK12492 331 DFSALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSPVASTNP-YGE---LARLGTV--GIPVPGTALKVIDDDG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 792 HPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIAdpfapgERMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGE 871
Cdd:PRK12492 405 NELPLGERGELCIKGPQVMKGYWQQPEATAEALDA------EGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNE 478
|
490
....*....|.
gi 16128569 872 IDRVMQALPDV 882
Cdd:PRK12492 479 IEDVVMAHPKV 489
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
481-846 |
1.08e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 72.24 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 481 FSYREMREQVVALANLLRERGVKPGDSVAVALP-RSVFLTLAlHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITT 559
Cdd:PRK08276 12 VTYGELEARSNRLAHGLRALGLREGDVVAILLEnNPEFFEVY-WAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIVS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 560 ddqlPRFSDV--------PNLTSLCYNAPLTPQGSAPLQLSQPHHTAYII----------FTSGSTGRPKGVM-----VG 616
Cdd:PRK08276 91 ----AALADTaaelaaelPAGVPLLLVVAGPVPGFRSYEEALAAQPDTPIadetagadmlYSSGTTGRPKGIKrplpgLD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 617 QTAIVNRLLWMQNHYPLTGEDVVAQKT-------PCSFDVSVWEFfwpfiaGAKLVMAEpeaHRDPLAMQQFFAEYGVTT 689
Cdd:PRK08276 167 PDEAPGMMLALLGFGMYGGPDSVYLSPaplyhtaPLRFGMSALAL------GGTVVVME---KFDAEEALALIERYRVTH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 690 THFVPSMlaaFVASLT-PQTARQS--CATLKQVFCSGEALPADLCR---EWQqltGAPLHNLYGPTEAAvDVSWypAFGE 763
Cdd:PRK08276 238 SQLVPTM---FVRMLKlPEEVRARydVSSLRVAIHAAAPCPVEVKRamiDWW---GPIIHEYYASSEGG-GVTV--ITSE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 764 ELAQVRGSsvpIGYPvWNTGLRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIadpfapGERMYRTGDVAr 843
Cdd:PRK08276 309 DWLAHPGS---VGKA-VLGEVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARN------PHGWVTVGDVG- 377
|
...
gi 16128569 844 WLD 846
Cdd:PRK08276 378 YLD 380
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
453-846 |
1.39e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 72.00 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 453 PETTLSALVAEQAAKTPDAPALA------DARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIV 526
Cdd:PRK12582 47 YPRSIPHLLAKWAAEAPDRPWLAqrepghGQWRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAM 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 527 EAGAAWLPLDTGYP-----DDRLKMMLEDARPSLLITTDDQL-------PRFSDVPNLT---------SLCYNA----PL 581
Cdd:PRK12582 127 QAGVPAAPVSPAYSlmshdHAKLKHLFDLVKPRVVFAQSGAPfaralaaLDLLDVTVVHvtgpgegiaSIAFADlaatPP 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 582 TPQGSAPLQLSQPHHTAYIIFTSGSTGRPKGV------MVGQTA-------------IVNRLLWMQNHYPLTGEdvvaqk 642
Cdd:PRK12582 207 TAAVAAAIAAITPDTVAKYLFTSGSTGMPKAVintqrmMCANIAmqeqlrprepdppPPVSLDWMPWNHTMGGN------ 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 643 tpCSFDVSVWEFFWPFIAGAKlvmaepeahrdPLAMQqfFAE-----YGVTTTHF--VPSMLAAFVASLT--PQTARQSC 713
Cdd:PRK12582 281 --ANFNGLLWGGGTLYIDDGK-----------PLPGM--FEEtirnlREISPTVYgnVPAGYAMLAEAMEkdDALRRSFF 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 714 ATLKQVFCSGEALPADLCREWQQLTGA------PLHNLYGPTEAA---VDVSWYPafgEELAQvrgssvpIGYPVWNTGL 784
Cdd:PRK12582 346 KNLRLMAYGGATLSDDLYERMQALAVRttghriPFYTGYGATETApttTGTHWDT---ERVGL-------IGLPLPGVEL 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128569 785 RIldammhpVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermYRTGDVARWLD 846
Cdd:PRK12582 416 KL-------APVGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGF------YRLGDAARFVD 464
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
4-200 |
2.85e-12 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380471 [Multi-domain] Cd Length: 430 Bit Score: 70.37 E-value: 2.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 4 HLPLVAAQPGIWMAEKLSELPSAWSVAHYVELTGEVDSPLLARAVVAGLAQADTLRMRFTEDNGEVWQWVDDALTFELPe 83
Cdd:cd20483 1 PRPMSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDPSFHLI- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 84 IIDLRTNIDPHGTAQALMQADLQQDLRVDSGKpLVFHQLIQVADNRWYWYQRYHHLLVDGFSFPAITRQIANIYCTWLRG 163
Cdd:cd20483 80 VIDLSEAADPEAALDQLVRNLRRQELDIEEGE-VIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALRAG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16128569 164 EPT---PASPFTpFADVVEEYQQYRESEAWQRDAAFWAEQ 200
Cdd:cd20483 159 RDLatvPPPPVQ-YIDFTLWHNALLQSPLVQPLLDFWKEK 197
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
470-886 |
5.01e-12 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 69.71 E-value: 5.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 470 DAPALADARYLFSYREMREQVVALANLLRE---RGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKM 546
Cdd:cd05929 4 RDLDRAQVFHQRRLLLLDVYSIALNRNARAaaaEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAEACA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 547 MLE---DARPSLLITTDDQLPRFSDVPNLTSLcynAPLTPqgSAPLQLsqphhTAYIIFTSGSTGRPKGVMVGQTA--IV 621
Cdd:cd05929 84 IIEikaAALVCGLFTGGGALDGLEDYEAAEGG---SPETP--IEDEAA-----GWKMLYSGGTTGRPKGIKRGLPGgpPD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 622 NRLLWM-QNHYPLTGEDVVAQKTPCSFDVSVWEFFWPFIAGAKLVMAEpeaHRDPLAMQQFFAEYGVTTTHFVPSMLAAF 700
Cdd:cd05929 154 NDTLMAaALGFGPGADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLME---KFDPEEFLRLIERYRVTFAQFVPTMFVRL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 701 VASLTPQTARQSCATLKQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAaVDVSWYPafGEELAQVRGSsvpIGYPVw 780
Cdd:cd05929 231 LKLPEAVRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTEG-QGLTIIN--GEEWLTHPGS---VGRAV- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 781 NTGLRILDAMMHPVPPGVAGDLYLTGiQLAQGYLGRPDLTASRFIADPFAPgermyrTGDVArWLDNGAVEYLG-RSDDQ 859
Cdd:cd05929 304 LGKVHILDEDGNEVPPGEIGEVYFAN-GPGFEYTNDPEKTAAARNEGGWST------LGDVG-YLDEDGYLYLTdRRSDM 375
|
410 420
....*....|....*....|....*..
gi 16128569 860 LKIRGQRIELGEIDRVMQALPDVEQAV 886
Cdd:cd05929 376 IISGGVNIYPQEIENALIAHPKVLDAA 402
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
482-905 |
5.68e-12 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 70.18 E-value: 5.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 482 SYREMREQVVALANLLR-ERGVKPGDSVAVALPRSV-FLTLALhAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITT 559
Cdd:cd17632 69 TYAELWERVGAVAAAHDpEQPVRPGDFVAVLGFTSPdYATVDL-ALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVS 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 560 DDQLP------------------------------------RFSDVPNLTSLCYNAPLTPQGSAPLQLSQPHHT----AY 599
Cdd:cd17632 148 AEHLDlaveavleggtpprlvvfdhrpevdahraalesareRLAAVGIPVTTLTLIAVRGRDLPPAPLFRPEPDddplAL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 600 IIFTSGSTGRPKGVMVGQTAIVNRLLWM---QNHYPLTGedVVAQKTPCSfdvSVWEFFWPFIAGAKLVMAEPEAHRDpl 676
Cdd:cd17632 228 LIYTSGSTGTPKGAMYTERLVATFWLKVssiQDIRPPAS--ITLNFMPMS---HIAGRISLYGTLARGGTAYFAAASD-- 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 677 aMQQFFAEYGV---TTTHFVP------------SMLAAFVASLTPQT-ARQSCATLKQV---------FCSGEALPADLC 731
Cdd:cd17632 301 -MSTLFDDLALvrpTELFLVPrvcdmlfqryqaELDRRSVAGADAETlAERVKAELRERvlggrllaaVCGSAPLSAEMK 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 732 REWQQLTGAPLHNLYGPTEAAV-----DVSWYPAFGEELAqvrgsSVP-IGYpvwntglrILDAMMHPvppgvAGDLYLT 805
Cdd:cd17632 380 AFMESLLDLDLHDGYGSTEAGAvildgVIVRPPVLDYKLV-----DVPeLGY--------FRTDRPHP-----RGELLVK 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 806 GIQLAQGYLGRPDLTASRFIADPFapgermYRTGDVARWLDNGAVEYLGRSDDQLKI-RGQRIELGEIDRVMQALPDVEQ 884
Cdd:cd17632 442 TDTLFPGYYKRPEVTAEVFDEDGF------YRTGDVMAELGPDRLVYVDRRNNVLKLsQGEFVTVARLEAVFAASPLVRQ 515
|
490 500 510
....*....|....*....|....*....|.
gi 16128569 885 AVTHA----------CVINQAAATGGDARQL 905
Cdd:cd17632 516 IFVYGnserayllavVVPTQDALAGEDTARL 546
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
15-250 |
5.70e-12 |
|
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380457 [Multi-domain] Cd Length: 428 Bit Score: 69.59 E-value: 5.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 15 WMAEKLSELPSAWSVAHYVELTGEVDSPLLARAVVAGLAQADTLRMRFTEDNGEVWQWV--DDALTFELpEIIDLRTNID 92
Cdd:cd19534 10 WFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIrgDVEELFRL-EVVDLSSLAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 93 PHGTAQALmqADLQQDLRVDSGkPLVFHQLIQVADNRwywyQRY----HHLLVDGFSFPAITRQIANIYCTWLRGEPTPA 168
Cdd:cd19534 89 AAAIEALA--AEAQSSLDLEEG-PLLAAALFDGTDGG----DRLllviHHLVVDGVSWRILLEDLEAAYEQALAGEPIPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 169 SPFTPFADVVEEYQQYRESEAWQRDAAFWAEQRRQLPPPASLSPAPLPGRSASadilrLKLEFTDGEFRQLATQLSGVQR 248
Cdd:cd19534 162 PSKTSFQTWAELLAEYAQSPALLEELAYWRELPAADYWGLPKDPEQTYGDART-----VSFTLDEEETEALLQEANAAYR 236
|
..
gi 16128569 249 TD 250
Cdd:cd19534 237 TE 238
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
6-200 |
6.28e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 70.76 E-value: 6.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 6 PLVAAQPGiWMAEKLSElPSAWSVAHYVELTGEVDSPLLARAVVAGLAQADTLRMRFTEDNGevwQWVDDALTFELPEII 85
Cdd:PRK12316 3640 LLLPIQQQ-FFEEPVPE-RHHWNQSLLLKPREALDAAALEAALQALVEHHDALRLRFVEDAG---GWTAEHLPVELGGAL 3714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 86 DLRTNIDPHGTAQALMQAdLQQDLRVDSGkPLVFHQLIQVADNRWYWYQRYHHLLVDGFSFPAITRQIANIYCTWLRGEP 165
Cdd:PRK12316 3715 LWRAELDDAEELERLGEE-AQRSLDLADG-PLLRALLATLADGSQRLLLVIHHLVVDGVSWRILLEDLQQAYQQLLQGEA 3792
|
170 180 190
....*....|....*....|....*....|....*..
gi 16128569 166 T--PASPfTPFADVVEEYQQYRESEAWQRDAAFWAEQ 200
Cdd:PRK12316 3793 PrlPAKT-SSFKAWAERLQEHARGEALKAELAYWQEQ 3828
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
6-200 |
8.07e-12 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380455 [Multi-domain] Cd Length: 421 Bit Score: 69.02 E-value: 8.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 6 PLVAAQPGIWMAEKLSELPSAWSVAHYVELTGEVDSPLLARAVVAGLAQADTLRMRF--TEDNGEVWQWVDDALTFELpE 83
Cdd:cd19532 3 PMSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFftDPEDGEPMQGVLASSPLRL-E 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 84 IIdlrtNIDPHGTAQALMQAdLQQ---DLrvDSGKPLVFhQLIQVADNRWYWYQRYHHLLVDGFSFPAITRQIANIYctw 160
Cdd:cd19532 82 HV----QISDEAEVEEEFER-LKNhvyDL--ESGETMRI-VLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAY--- 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16128569 161 lRGEPTPASPfTPFADVVEEYQQYRESEAWQRDAAFWAEQ 200
Cdd:cd19532 151 -NGQPLLPPP-LQYLDFAARQRQDYESGALDEDLAYWKSE 188
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
31-424 |
8.34e-12 |
|
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380465 [Multi-domain] Cd Length: 423 Bit Score: 68.77 E-value: 8.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 31 HYVE-----LTGEVDSPLLARAVVAGLAQADTLRMRFT-EDNGEVWQWVDDALTFELpEIIDLR--TNIDPHGTAQALMQ 102
Cdd:cd19543 23 AYVEqmvitLEGPLDPDRFRAAWQAVVDRHPILRTSFVwEGLGEPLQVVLKDRKLPW-RELDLShlSEAEQEAELEALAE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 103 ADLQQ--DLRVDsgkPLVFHQLIQVADNRWYWYQRYHHLLVDGFSFPAITRQIANIYCTWLRGEPTPASPFTPFADvvee 180
Cdd:cd19543 102 EDRERgfDLARA---PLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALGEGQPPSLPPVRPYRD---- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 181 YQQYREseawQRDA----AFWAEQRRQLPPPASLSPAPLPGRSASADILRLKLEF---TDGEFRQLATQ----LSGVQRT 249
Cdd:cd19543 175 YIAWLQ----RQDKeaaeAYWREYLAGFEEPTPLPKELPADADGSYEPGEVSFELsaeLTARLQELARQhgvtLNTVVQG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 250 dlalalaaLW---LGRLCNRMDYAAGFIFMRRlgSAAL----TATGPVLNVLPLGIHIAAQETLPELATRLAAQLKKMRR 322
Cdd:cd19543 251 --------AWallLSRYSGRDDVVFGTTVSGR--PAELpgieTMVGLFINTLPVRVRLDPDQTVLELLKDLQAQQLELRE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 323 HQRYDAEQIvrdSGRAAGDEPLFGpvlNIKVFD-Y-------------QLDIPDVQAQTHTlatgpvN-DLELALFPDvh 387
Cdd:cd19543 321 HEYVPLYEI---QAWSEGKQALFD---HLLVFEnYpvdesleeeqdedGLRITDVSAEEQT------NyPLTVVAIPG-- 386
|
410 420 430
....*....|....*....|....*....|....*..
gi 16128569 388 GDLSIEILANKQRYDEPTLIQHAERLKMLIAQFAADP 424
Cdd:cd19543 387 EELTIKLSYDAEVFDEATIERLLGHLRRVLEQVAANP 423
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
481-931 |
9.61e-12 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 69.00 E-value: 9.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 481 FSYREMREQVVALANLLR-ERGVKPGDSVAVALPRS---VFLTLALHAIveaGAAWLPLDTGYPDDRLKMMLEDARPSLL 556
Cdd:cd05937 6 WTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSpefVFLWLGLWSI---GAAPAFINYNLSGDPLIHCLKLSGSRFV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 557 ITTDDQLprfsdvpnltslcynapltpqgsaplqlsqphhtAYIIFTSGSTGRPKGVmvgqtAIVNRLLW-----MQNHY 631
Cdd:cd05937 83 IVDPDDP----------------------------------AILIYTSGTTGLPKAA-----AISWRRTLvtsnlLSHDL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 632 PLTGEDVVAQKTPCSFDVSvweFFWPFIA----GAKLVMAEPEAHRdplamqQFFAE-YGVTTTHFVpsmlaaFVASL-- 704
Cdd:cd05937 124 NLKNGDRTYTCMPLYHGTA---AFLGACNclmsGGTLALSRKFSAS------QFWKDvRDSGATIIQ------YVGELcr 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 705 ----TPQTARQSCATLKQVFcsGEALPADLCREWQQLTGAP-LHNLYGPTEA--AVDVSWYPAFGEELAQVRGS------ 771
Cdd:cd05937 189 yllsTPPSPYDRDHKVRVAW--GNGLRPDIWERFRERFNVPeIGEFYAATEGvfALTNHNVGDFGAGAIGHHGLirrwkf 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 772 ---SVPIGYPVwNTGLRILD-----AMMHPV-PPG-VAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDV 841
Cdd:cd05937 267 enqVVLVKMDP-ETDDPIRDpktgfCVRAPVgEPGeMLGRVPFKNREAFQGYLHNEDATESKLVRDVFRKGDIYFRTGDL 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 842 ARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQAVTHACvinQAAATGGDARQLVGYLVSQSGLP--LDT 919
Cdd:cd05937 346 LRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGV---KVPGHDGRAGCAAITLEESSAVPteFTK 422
|
490
....*....|..
gi 16128569 920 SALQAQLRETLP 931
Cdd:cd05937 423 SLLASLARKNLP 434
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
465-886 |
1.01e-11 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 69.21 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 465 AAKTPDAPAL------ADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALP---RSVFLTL------ALHAIVEAG 529
Cdd:PRK10524 63 LAKRPEQLALiavsteTDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPmiaEAAFAMLacarigAIHSVVFGG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 530 AAwlpldtgypDDRLKMMLEDARPSLLITTD---------------DQLPRFSDVPNLTSLCYNAPLTPQ---------- 584
Cdd:PRK10524 143 FA---------SHSLAARIDDAKPVLIVSADagsrggkvvpykpllDEAIALAQHKPRHVLLVDRGLAPMarvagrdvdy 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 585 ---------GSAPLQLSQPHHTAYIIFTSGSTGRPKGVM--VGQTAIvnrllwmqnhypltgedVVAQKTPCSFDVSVWE 653
Cdd:PRK10524 214 atlraqhlgARVPVEWLESNEPSYILYTSGTTGKPKGVQrdTGGYAV-----------------ALATSMDTIFGGKAGE 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 654 FFW-----------------PFIAGAKLVMAEPEAHR-DPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPQTARQSCAT 715
Cdd:PRK10524 277 TFFcasdigwvvghsyivyaPLLAGMATIMYEGLPTRpDAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDPALLRKHDLSS 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 716 LKQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEaavdvSWYPAfgeeLAQVRG-SSVPI-----GYPVWNTGLRILD- 788
Cdd:PRK10524 357 LRALFLAGEPLDEPTASWISEALGVPVIDNYWQTE-----TGWPI----LAIARGvEDRPTrlgspGVPMYGYNVKLLNe 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 789 AMMHPVPPGVAGDLYLTGiQLAQGYLG---RPDltaSRFIADPF-APGERMYRTGDVARWLDNGAVEYLGRSDDQLKIRG 864
Cdd:PRK10524 428 VTGEPCGPNEKGVLVIEG-PLPPGCMQtvwGDD---DRFVKTYWsLFGRQVYSTFDWGIRDADGYYFILGRTDDVINVAG 503
|
490 500
....*....|....*....|...
gi 16128569 865 QRIELGEIDRVMQALPDV-EQAV 886
Cdd:PRK10524 504 HRLGTREIEESISSHPAVaEVAV 526
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
600-892 |
1.03e-11 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 67.68 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 600 IIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTGEDVVAQKTPCsFDVS-VWEFFWPFIAGAKLVMAEpeaHRDPLAM 678
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPL-FHIAgLNLALATFHAGGANVVME---KFDPAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 679 QQFFAEYGVTTTHFVPSMLAAFVASLTPQTArqSCATLKQVfcSGEALPADLCReWQQLTGAPLHNLYGPTEAAVDVSWY 758
Cdd:cd17637 81 LELIEEEKVTLMGSFPPILSNLLDAAEKSGV--DLSSLRHV--LGLDAPETIQR-FEETTGATFWSLYGQTETSGLVTLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 759 PAFGeelaqvRGSSVpiGYPVWNTGLRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFiadpfapgeR--MY 836
Cdd:cd17637 156 PYRE------RPGSA--GRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF---------RngWH 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 16128569 837 RTGDVARWLDNGAVEYLGRS--DDQLKIRGQRIELGEIDRVMQALPDVEQavthACVI 892
Cdd:cd17637 219 HTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAE----VCVI 272
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
481-933 |
1.24e-11 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 68.86 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 481 FSYREMREQVVALAN-LLRERGVKPGDSVAVALPRS-----VFLTLA------------------LHAIVEAGAAWLPLD 536
Cdd:cd05938 6 YTYRDVDRRSNQAARaLLAHAGLRPGDTVALLLGNEpaflwIWLGLAklgcpvaflntnirskslLHCFRCCGAKVLVVA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 537 tgyPDdrLKMMLEDARPSLlitTDDQ-----LPRFSDVPNLTSLCYNAPLTPQGSAPLQLSQPHH---TAYIIFTSGSTG 608
Cdd:cd05938 86 ---PE--LQEAVEEVLPAL---RADGvsvwyLSHTSNTEGVISLLDKVDAASDEPVPASLRAHVTiksPALYIYTSGTTG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 609 RPKGVMVGQTaivnRLLWMQNHYPLTG---EDVVAQKTPCSFDV-SVWEFFWPFIAGAKLVMaepeahRDPLAMQQFFAE 684
Cdd:cd05938 158 LPKAARISHL----RVLQCSGFLSLCGvtaDDVIYITLPLYHSSgFLLGIGGCIELGATCVL------KPKFSASQFWDD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 685 ---YGVTTTHFVPSMLAAFVAslTPQTARQSCATLKQVFCSGeaLPADLCREWQQLTGaPLH--NLYGPTEAAVDVSWYP 759
Cdd:cd05938 228 crkHNVTVIQYIGELLRYLCN--QPQSPNDRDHKVRLAIGNG--LRADVWREFLRRFG-PIRirEFYGSTEGNIGFFNYT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 760 afGEELAQVRGSS-----VP---IGYPVwNTGLRILDAMMH--PVPPGVAGdLYLTGIQLAQ---GYLGRPDLTASRFIA 826
Cdd:cd05938 303 --GKIGAVGRVSYlykllFPfelIKFDV-EKEEPVRDAQGFciPVAKGEPG-LLVAKITQQSpflGYAGDKEQTEKKLLR 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 827 DPFAPGERMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQA-VTHACVINQAAATGGDARQL 905
Cdd:cd05938 379 DVFKKGDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVnVYGVTVPGHEGRIGMAAVKL 458
|
490 500
....*....|....*....|....*...
gi 16128569 906 vgylvsQSGLPLDTSALQAQLRETLPPH 933
Cdd:cd05938 459 ------KPGHEFDGKKLYQHVREYLPAY 480
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
453-930 |
1.28e-11 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 69.05 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 453 PETTLSalVAEQA--AKTPDAPAL-----ADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALP---RSVFLTLAL 522
Cdd:PRK03584 82 PGARLN--YAENLlrHRRDDRPAIifrgeDGPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPnipETVVAMLAT 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 523 HAIveaGAAWlplDTGYPD-------DRLKMMledaRPSLLITTD-------------------DQLPRFSD---VPNLT 573
Cdd:PRK03584 160 ASL---GAIW---SSCSPDfgvqgvlDRFGQI----EPKVLIAVDgyryggkafdrrakvaelrAALPSLEHvvvVPYLG 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 574 S----------LCYNAPLTPQGSAPLQLSQ--PHHTAYIIFTSGSTGRPKGVMVGQTAIV-NRLLWMQNHYPLTGEDVVA 640
Cdd:PRK03584 230 PaaaaaalpgaLLWEDFLAPAEAAELEFEPvpFDHPLWILYSSGTTGLPKCIVHGHGGILlEHLKELGLHCDLGPGDRFF 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 641 QKTPCSfdvsvWeFFWPFIA-----GAKLVMAE--PeAHRDPLAMQQFFAEYGVTttHFVPSmlAAFVAS-----LTP-Q 707
Cdd:PRK03584 310 WYTTCG-----W-MMWNWLVsgllvGATLVLYDgsP-FYPDPNVLWDLAAEEGVT--VFGTS--AKYLDAcekagLVPgE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 708 TARQScaTLKQVFCSGEALPAD----LCREWQQ-----------------LTGAPLHNLYgPTE-------AAVDVsWYP 759
Cdd:PRK03584 379 THDLS--ALRTIGSTGSPLPPEgfdwVYEHVKAdvwlasisggtdicscfVGGNPLLPVY-RGEiqcrglgMAVEA-WDE 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 760 AfGEELAQVRGS--------SVPIGYpvWN--TGLRILDAmmhpvppgvagdlyltgiqlaqgYLgrpdltaSRFiadpf 829
Cdd:PRK03584 455 D-GRPVVGEVGElvctkpfpSMPLGF--WNdpDGSRYRDA-----------------------YF-------DTF----- 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 830 aPGerMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQAVthacVINQAAAtGGDARqLVGYL 909
Cdd:PRK03584 497 -PG--VWRHGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSL----VIGQEWP-DGDVR-MPLFV 567
|
570 580
....*....|....*....|.
gi 16128569 910 VSQSGLPLDtSALQAQLRETL 930
Cdd:PRK03584 568 VLAEGVTLD-DALRARIRTTI 587
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
4-424 |
2.86e-11 |
|
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380462 [Multi-domain] Cd Length: 427 Bit Score: 67.40 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 4 HLPLVAAQPGIWMAEKLSELPSAWSVAHYVELTGEVDSPLLARAVVAGLAQADTLRMRFT-EDNGEVWQWVDDALTFELP 82
Cdd:cd19539 1 RIPLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVrDDGGVPRQEILPPGPAPLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 83 EIIDLRTNIDPhgTAQALMQADLQQDLRVD-SGKPLVFHQLIQVADNRWYWYQRYHHLLVDGFSFPAITRQIANIYCTwL 161
Cdd:cd19539 81 VRDLSDPDSDR--ERRLEELLRERESRGFDlDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAA-R 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 162 RGEPTPASPFTPfadvveeyQQYRESEAWQRDA----------AFWaeqRRQLPPPASLSPAPLPGRSASADILRLKLEF 231
Cdd:cd19539 158 RKGPAAPLPELR--------QQYKEYAAWQREAlaapraaellDFW---RRRLRGAEPTALPTDRPRPAGFPYPGADLRF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 232 -TDGEFRQLATQLSGVQRTDLALALAALW---LGRLCNRMDYAAGFIFMRRLGSAALTATGPVLNVLPLGIHIAAQETLP 307
Cdd:cd19539 227 eLDAELVAALRELAKRARSSLFMVLLAAYcvlLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 308 ELATRLAAQLKKMRRHQRYDAEQIVRDSG--RAAGDEPLFGPVLNIKVF-DYQLDIPDVQAQTHTLATGPVNDLELALFP 384
Cdd:cd19539 307 DLIARVRKALVDAQRHQELPFQQLVAELPvdRDAGRHPLVQIVFQVTNApAGELELAGGLSYTEGSDIPDGAKFDLNLTV 386
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 16128569 385 -DVHGDLSIEILANKQRYDEPTLIQHAERLKMLIAQFAADP 424
Cdd:cd19539 387 tEEGTGLRGSLGYATSLFDEETIQGFLADYLQVLRQLLANP 427
|
|
| GrsT |
COG3208 |
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ... |
1065-1192 |
2.70e-10 |
|
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442441 [Multi-domain] Cd Length: 237 Bit Score: 62.18 E-value: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 1065 GPTLFCFHPASGFAWQFSVLSRYLDPQWSIIGIQSP----RPNGPMqtAANLDEVCEAhLATLLEQQPHGPYYLLGYSLG 1140
Cdd:COG3208 6 RLRLFCFPYAGGSASAYRPWAAALPPDIEVLAVQLPgrgdRLGEPP--LTSLEELADD-LAEELAPLLDRPFALFGHSMG 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 16128569 1141 GTLAQGIAARLRARGeQVAFLGL-LDTWPPETQNWQEKEANGL-DPEVLAEINR 1192
Cdd:COG3208 83 ALLAFELARRLERRG-RPLPAHLfVSGRRAPHLPRRRRPLHDLsDAELLAELRR 135
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
447-864 |
4.90e-10 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 63.68 E-value: 4.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 447 ATQVEIPETTLSALVAEQAAKTPDAPAL--ADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHA 524
Cdd:PRK08315 8 PTDVPLLEQTIGQLLDRTAARYPDREALvyRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 525 IVEAGA-----------------------AWLPLDTGYPDDRLKMMLEDARPSL------------------LITTDDQL 563
Cdd:PRK08315 88 TAKIGAilvtinpayrlseleyalnqsgcKALIAADGFKDSDYVAMLYELAPELatcepgqlqsarlpelrrVIFLGDEK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 564 PR----FSDVPNLTSLCYNAPLTPQGSaplQLsQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTGEDVV 639
Cdd:PRK08315 168 HPgmlnFDELLALGRAVDDAELAARQA---TL-DPDDPINIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 640 AQKTPcsfdvsvweFFWPF----------IAGAKLVMAEPEAhrDPLAMQQFFAEYGVTTTHFVPSMlaaFVASLT-PQT 708
Cdd:PRK08315 244 CIPVP---------LYHCFgmvlgnlacvTHGATMVYPGEGF--DPLATLAAVEEERCTALYGVPTM---FIAELDhPDF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 709 ARQSCATLKQVFCSGEALPADLCREWQ------QLTGAplhnlYGPTEAAvDVSWYPAFGEELaQVRGSSVpiGYPVWNT 782
Cdd:PRK08315 310 ARFDLSSLRTGIMAGSPCPIEVMKRVIdkmhmsEVTIA-----YGMTETS-PVSTQTRTDDPL-EKRVTTV--GRALPHL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 783 GLRILDAMMH-PVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgerMyRTGDVARWLDNGAVEYLGRSDDQLk 861
Cdd:PRK08315 381 EVKIVDPETGeTVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGW-----M-HTGDLAVMDEEGYVNIVGRIKDMI- 453
|
...
gi 16128569 862 IRG 864
Cdd:PRK08315 454 IRG 456
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
451-890 |
7.83e-10 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 63.10 E-value: 7.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 451 EIPETTLSALVaEQAAKTPDAPAL--ADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEA 528
Cdd:PRK05857 11 QLPSTVLDRVF-EQARQQPEAIALrrCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 529 GAAWLPLDTGYPDDRLKMMLEDARPSLLITTDDQLPRFSDVP-----------NLTSLCYNAPLTPQGSAPLqlSQPHHT 597
Cdd:PRK05857 90 GAIAVMADGNLPIAAIERFCQITDPAAALVAPGSKMASSAVPealhsipviavDIAAVTRESEHSLDAASLA--GNADQG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 598 A----YIIFTSGSTGRPKGVMvgqtaIVNRLLW----MQNHYPLTGEDVVAQKT-----PCSFDVSVWEFFWPFIAGAKL 664
Cdd:PRK05857 168 SedplAMIFTSGTTGEPKAVL-----LANRTFFavpdILQKEGLNWVTWVVGETtysplPATHIGGLWWILTCLMHGGLC 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 665 VMAEPEAhrdpLAMQQFFAEYGVTTTHFVPSMLAAFVASLtpQTARQSCATLKQVFCSG-EALPADLcrEWQQLTGAPLH 743
Cdd:PRK05857 243 VTGGENT----TSLLEILTTNAVATTCLVPTLLSKLVSEL--KSANATVPSLRLVGYGGsRAIAADV--RFIEATGVRTA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 744 NLYGPTEAAVDVSWYPAFGEELAQVRGSSVPIGYPVWNTGLRILDAmMHPVPPGVA-----GDLYLTGIQLAQGYLGRPD 818
Cdd:PRK05857 315 QVYGLSETGCTALCLPTDDGSIVKIEAGAVGRPYPGVDVYLAATDG-IGPTAPGAGpsasfGTLWIKSPANMLGYWNNPE 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128569 819 LTASRFIadpfapgERMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQAvthAC 890
Cdd:PRK05857 394 RTAEVLI-------DGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREA---AC 455
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
482-882 |
9.88e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 62.71 E-value: 9.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 482 SYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLED--ARPSLLITT 559
Cdd:PRK07768 31 TWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPRTDLAVWAEDtlRVIGMIGAK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 560 --------DDQLPRFSD----VPNLTSLCYNAPLTPQgsaplqLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWM 627
Cdd:PRK07768 111 avvvgepfLAAAPVLEEkgirVLTVADLLAADPIDPV------ETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAM 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 628 QNHYPLTGE-DVVAQKTPCSFDVSVWEFFW-PFIAGAKLVMAEP-EAHRDPLAMQQFFAEYGVTTT---HFVPSMLAAFV 701
Cdd:PRK07768 185 FVAAEFDVEtDVMVSWLPLFHDMGMVGFLTvPMYFGAELVKVTPmDFLRDPLLWAELISKYRGTMTaapNFAYALLARRL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 702 ASLTPQtARQSCATLKQVFCSGEAL-PA---DLCREwqqltGAPlHNL--------YGPTEAAVDVSwYPAFGE------ 763
Cdd:PRK07768 265 RRQAKP-GAFDLSSLRFALNGAEPIdPAdveDLLDA-----GAR-FGLrpeailpaYGMAEATLAVS-FSPCGAglvvde 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 764 ---ELAQVRGSSVP-----------IGYPVWNTGLRILDAMMHPVPPGVAGDLYLTGIQLAQGYlgrpdLTASRFIADPF 829
Cdd:PRK07768 337 vdaDLLAALRRAVPatkgntrrlatLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGY-----LTMDGFIPAQD 411
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 16128569 830 APGerMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDV 882
Cdd:PRK07768 412 ADG--WLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGV 462
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
452-885 |
1.33e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 62.27 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 452 IPETTLSALvaEQAAKT-PDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGA 530
Cdd:PRK08162 16 VPLTPLSFL--ERAAEVyPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 531 AWLPLDTGYPDDRLKMMLEDARPSLLIT----------------------TDDQLPRFSDVPNLTSLCYNAPLTpQGSAP 588
Cdd:PRK08162 94 VLNTLNTRLDAASIAFMLRHGEAKVLIVdtefaevarealallpgpkplvIDVDDPEYPGGRFIGALDYEAFLA-SGDPD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 589 LQLSQPHHTAYII---FTSGSTGRPKGVMVGQ-----TAIVNRLLW-MQNH--Y----PLtgedvvaqktpcsFDVSVWE 653
Cdd:PRK08162 173 FAWTLPADEWDAIalnYTSGTTGNPKGVVYHHrgaylNALSNILAWgMPKHpvYlwtlPM-------------FHCNGWC 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 654 FFWPFIAGA-------KLvmaepeahrDPLAMQQFFAEYGVttTHF-----VPSMLAAfvaslTPQTARQSCATLKQVFC 721
Cdd:PRK08162 240 FPWTVAARAgtnvclrKV---------DPKLIFDLIREHGV--THYcgapiVLSALIN-----APAEWRAGIDHPVHAMV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 722 SGEALPADLCREWQQLtGAPLHNLYGPTE----AAVdVSWYPAFGE----ELAQVRG-SSVPigYPVwNTGLRILD-AMM 791
Cdd:PRK08162 304 AGAAPPAAVIAKMEEI-GFDLTHVYGLTEtygpATV-CAWQPEWDAlpldERAQLKArQGVR--YPL-QEGVTVLDpDTM 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 792 HPVPPG--VAGDLYLTGIQLAQGYLGRPDLTasrfiADPFAPGerMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIEL 869
Cdd:PRK08162 379 QPVPADgeTIGEIMFRGNIVMKGYLKNPKAT-----EEAFAGG--WFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISS 451
|
490
....*....|....*.
gi 16128569 870 GEIDRVMQALPDVEQA 885
Cdd:PRK08162 452 IEVEDVLYRHPAVLVA 467
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
599-930 |
1.35e-09 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 61.63 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 599 YIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNH---YPLTGEDVVAQKT-----------PCSFDVSVWEFFWPFIAGAKL 664
Cdd:cd05924 7 YILYTGGTTGMPKGVMWRQEDIFRMLMGGADFgtgEFTPSEDAHKAAAaaagtvmfpapPLMHGTGSWTAFGGLLGGQTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 665 VMaePEAHRDPLAMQQFFAEYGVTTTHFV-PSMLAAFVASLTPQTARqSCATLKQVFCSGEALP----ADLCREWQQLTg 739
Cdd:cd05924 87 VL--PDDRFDPEEVWRTIEKHKVTSMTIVgDAMARPLIDALRDAGPY-DLSSLFAISSGGALLSpevkQGLLELVPNIT- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 740 apLHNLYGPTEAAVDVSWYPAFGEELAQVRGSSVPigypvwntGLRILDAMMHPVPPGVAGdlyltGIQLAQ------GY 813
Cdd:cd05924 163 --LVDAFGSSETGFTGSGHSAGSGPETGPFTRANP--------DTVVLDDDGRVVPPGSGG-----VGWIARrghiplGY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 814 LGRPDLTASRFiadPFAPGERMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQAVthacVIN 893
Cdd:cd05924 228 YGDEAKTAETF---PEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVL----VVG 300
|
330 340 350
....*....|....*....|....*....|....*..
gi 16128569 894 QAAATGGdaRQLVGYLVSQSGLPLDTSALQAQLRETL 930
Cdd:cd05924 301 RPDERWG--QEVVAVVQLREGAGVDLEELREHCRTRI 335
|
|
| PKS_TE |
smart00824 |
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide ... |
1109-1197 |
1.74e-09 |
|
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.
Pssm-ID: 214835 [Multi-domain] Cd Length: 212 Bit Score: 59.16 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 1109 AANLDEVCEAHLATLLEQQPHGPYYLLGYSLGGTLAQGIAARLRARGEQVAFLGLLDTWPPETQnwqekEANGLDPEVLA 1188
Cdd:smart00824 43 PASADALVEAQAEAVLRAAGGRPFVLVGHSSGGLLAHAVAARLEARGIPPAAVVLLDTYPPGDP-----APEGWLPELLR 117
|
....*....
gi 16128569 1189 EINREREAF 1197
Cdd:smart00824 118 GVFEREDSF 126
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
980-1036 |
2.46e-09 |
|
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 54.49 E-value: 2.46e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 16128569 980 IAAAFSSLLGCDVQ--DADADFFALGGHSLLAMKLAAQLSRQVARQVTPGQVMVASTVA 1036
Cdd:pfam00550 3 LRELLAEVLGVPAEeiDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLA 61
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
451-613 |
5.90e-09 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 60.28 E-value: 5.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 451 EIPETTLSALVaEQAAKTPDAPALADA------RYLfSYREMREQVVALANLLRERGVKPGDSVAVALPRSV-FLTLALH 523
Cdd:PRK08180 36 DYPRRLTDRLV-HWAQEAPDRVFLAERgadggwRRL-TYAEALERVRAIAQALLDRGLSAERPLMILSGNSIeHALLALA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 524 AIVeAGAAWLPLDTGY---PDD--RLKMMLEDARPSLLITTDDQL-------PRFSDVP-----------NLTSL--CYN 578
Cdd:PRK08180 114 AMY-AGVPYAPVSPAYslvSQDfgKLRHVLELLTPGLVFADDGAAfaralaaVVPADVEvvavrgavpgrAATPFaaLLA 192
|
170 180 190
....*....|....*....|....*....|....*
gi 16128569 579 APLTPQGSAPLQLSQPHHTAYIIFTSGSTGRPKGV 613
Cdd:PRK08180 193 TPPTAAVDAAHAAVGPDTIAKFLFTSGSTGLPKAV 227
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
461-846 |
8.57e-09 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 59.75 E-value: 8.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 461 VAEQAAKTPDAPALAD-----ARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPL 535
Cdd:cd05921 1 LAHWARQAPDRTWLAEregngGWRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 536 DTGY----PD-DRLKMMLEDARPSLLITTDDqlPRFSD------------------VPNLTSLCYNAPL-TPQGSAPLQL 591
Cdd:cd05921 81 SPAYslmsQDlAKLKHLFELLKPGLVFAQDA--APFARalaaifplgtplvvsrnaVAGRGAISFAELAaTPPTAAVDAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 592 ---SQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTGEDVvaqktPCSFDvsvWeFFWPFIAGAKLVMaE 668
Cdd:cd05921 159 faaVGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEP-----PVLVD---W-LPWNHTFGGNHNF-N 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 669 PEAHR-------DPLAMQQFFAE-----YGVTTTHF--VPSMLAAFVASLT--PQTARQSCATLKQVFCSGEALPADLCR 732
Cdd:cd05921 229 LVLYNggtlyidDGKPMPGGFEEtlrnlREISPTVYfnVPAGWEMLVAALEkdEALRRRFFKRLKLMFYAGAGLSQDVWD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 733 EWQQLTGA------PLHNLYGPTEAAVDVSwypaFGEELAQVRGSsvpIGYPVWNTGLRIldammhpVPPGVAGDLYLTG 806
Cdd:cd05921 309 RLQALAVAtvgeriPMMAGLGATETAPTAT----FTHWPTERSGL---IGLPAPGTELKL-------VPSGGKYEVRVKG 374
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 16128569 807 IQLAQGYLGRPDLTASRFIADPFapgermYRTGDVARWLD 846
Cdd:cd05921 375 PNVTPGYWRQPELTAQAFDEEGF------YCLGDAAKLAD 408
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
598-958 |
1.18e-08 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 58.52 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 598 AYIIFTSGSTGRPKGVMVGQTAIV--------------NRLLWMQNHYpLTG-----EDVVAQKTPCSFDVSVwEFFWPF 658
Cdd:PRK07824 38 ALVVATSGTTGTPKGAMLTAAALTasadathdrlggpgQWLLALPAHH-IAGlqvlvRSVIAGSEPVELDVSA-GFDPTA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 659 IAGAKLVMAEPEAHRDPLAMQqffaeygvttthfvpsmlaaFVASLTPQTARQSCATLKQVFCSGEALPADLCREWQQLt 738
Cdd:PRK07824 116 LPRAVAELGGGRRYTSLVPMQ--------------------LAKALDDPAATAALAELDAVLVGGGPAPAPVLDAAAAA- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 739 GAPLHNLYGPTEAAvdvswypafgeelaqvrGSSVPIGYPVWNTGLRILDammhpvppgvaGDLYLTGIQLAQGYLGRPD 818
Cdd:PRK07824 175 GINVVRTYGMSETS-----------------GGCVYDGVPLDGVRVRVED-----------GRIALGGPTLAKGYRNPVD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 819 ltasrfiADPFA-PGerMYRTGDVARwLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPdveqAVTHACVINQAaa 897
Cdd:PRK07824 227 -------PDPFAePG--WFRTDDLGA-LDDGVLTVLGRADDAISTGGLTVLPQVVEAALATHP----AVADCAVFGLP-- 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128569 898 tggDAR--QLVGYLVSQSGLPLDT-SALQAQLRETLPPHMVPVVLLQLPQLPLSANGKLDRKAL 958
Cdd:PRK07824 291 ---DDRlgQRVVAAVVGDGGPAPTlEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
478-891 |
1.47e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 58.95 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 478 RYlfSYREMREQVVALANLLRERGVKPGDSVAV----------------------------------------ALPRSVF 517
Cdd:PRK07008 39 RY--TYRDCERRAKQLAQALAALGVEPGDRVGTlawngyrhleayygvsgsgavchtinprlfpeqiayivnhAEDRYVL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 518 LTLALHAIVEAGAAWLPLDTGYpddrlkmmledarpsLLITTDDQLPRFSdVPnltSLCYNAPLTPQGSAPLQLSQPHHT 597
Cdd:PRK07008 117 FDLTFLPLVDALAPQCPNVKGW---------------VAMTDAAHLPAGS-TP---LLCYETLVGAQDGDYDWPRFDENQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 598 A-YIIFTSGSTGRPKGVMVGQTAIVnrLLWMQNHYP----LTGEDVVAQKTPCsFDVSVWEFfwPFIA---GAKLVMaeP 669
Cdd:PRK07008 178 AsSLCYTSGTTGNPKGALYSHRSTV--LHAYGAALPdamgLSARDAVLPVVPM-FHVNAWGL--PYSApltGAKLVL--P 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 670 EAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPQTARQScaTLKQVFCSGEALPADLCREWQQLTGAPLHNLYGPT 749
Cdd:PRK07008 251 GPDLDGKSLYELIEAERVTFSAGVPTVWLGLLNHMREAGLRFS--TLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 750 EAA-----VDVSW----YPafGEELAQVRGSSvpiGYPVWNTGLRILDAMMHPVP-PGVA-GDLYLTGIQLAQGYLGRPd 818
Cdd:PRK07008 329 EMSplgtlCKLKWkhsqLP--LDEQRKLLEKQ---GRVIYGVDMKIVGDDGRELPwDGKAfGDLQVRGPWVIDRYFRGD- 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128569 819 ltasrfiADPFAPGerMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQAvthACV 891
Cdd:PRK07008 403 -------ASPLVDG--WFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEA---ACI 463
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
469-969 |
2.90e-08 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 58.11 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 469 PDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMML 548
Cdd:PLN03102 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 549 EDARPSLL----------------ITTDDQLPR---------------FSDVPNLTSLCYNAPLTPQGSAPLQLSQPHHT 597
Cdd:PLN03102 108 RHAKPKILfvdrsfeplarevlhlLSSEDSNLNlpvifiheidfpkrpSSEELDYECLIQRGEPTPSLVARMFRIQDEHD 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 598 AYII-FTSGSTGRPKGVMVGQ-----TAIVNRLLWMQNHYPltgedvVAQKTPCSFDVSVWEFFWPFIA--GAKLVM--- 666
Cdd:PLN03102 188 PISLnYTSGTTADPKGVVISHrgaylSTLSAIIGWEMGTCP------VYLWTLPMFHCNGWTFTWGTAArgGTSVCMrhv 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 667 AEPEAHRDplamqqfFAEYGVTTTHFVPSMLAAFV-ASLTPQTARQSCAtlkQVFCSGEALPADLCREWQQLTGAPLHNl 745
Cdd:PLN03102 262 TAPEIYKN-------IEMHNVTHMCCVPTVFNILLkGNSLDLSPRSGPV---HVLTGGSPPPAALVKKVQRLGFQVMHA- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 746 YGPTEAAVDV---SWYPAFGE-------ELAQVRGSSvpigypvwNTGLRILDA----MMHPVPPG--VAGDLYLTGIQL 809
Cdd:PLN03102 331 YGLTEATGPVlfcEWQDEWNRlpenqqmELKARQGVS--------ILGLADVDVknkeTQESVPRDgkTMGEIVIKGSSI 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 810 AQGYLGRPDLTASRFiadpfapGERMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDV-EQAVTH 888
Cdd:PLN03102 403 MKGYLKNPKATSEAF-------KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVlETAVVA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 889 -----------ACVINQAAATGGDARqlVGYLVSQSGlpldtsALQAQLRETLPPHMVPVVLLQLPQLPLSANGKldrka 957
Cdd:PLN03102 476 mphptwgetpcAFVVLEKGETTKEDR--VDKLVTRER------DLIEYCRENLPHFMCPRKVVFLQELPKNGNGK----- 542
|
570
....*....|..
gi 16128569 958 LPLPELKAQAPG 969
Cdd:PLN03102 543 ILKPKLRDIAKG 554
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
453-889 |
4.00e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 57.73 E-value: 4.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 453 PETTLSALVAEQAakTPDAPALADARYLFSYREMREQVVALANLLRERGVKPGD-SVAVALPRSVFLTLALHAIVEAGAA 531
Cdd:PRK13388 1 MRDTIAQLLRDRA--GDDTIAVRYGDRTWTWREVLAEAAARAAALIALADPDRPlHVGVLLGNTPEMLFWLAAAALGGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 532 WLPLDtgyPDDRLKMMLEDARPS---LLITTDDQLPRFS--DVPNLTSLCYNAPLTPQGSAPLQLSQPH------HTAYI 600
Cdd:PRK13388 79 LVGLN---TTRRGAALAADIRRAdcqLLVTDAEHRPLLDglDLPGVRVLDVDTPAYAELVAAAGALTPHrevdamDPFML 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 601 IFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTGEDVVAQKTPCSFDVSVWEFFWPFIA-GAKLvmaepeAHRDPLAMQ 679
Cdd:PRK13388 156 IFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPAVAsGAAV------ALPAKFSAS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 680 QFFA---EYGVTTTHFVPSMLAAFVAslTPQTARQSCATLKQVFcSGEALPADLcREWQQLTGAPLHNLYGPTEAAVDVS 756
Cdd:PRK13388 230 GFLDdvrRYGATYFNYVGKPLAYILA--TPERPDDADNPLRVAF-GNEASPRDI-AEFSRRFGCQVEDGYGSSEGAVIVV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 757 WYPAFGEelaqvrGSsvpIGYPVwnTGLRILDA-MMHPVPPGV-------------AGDLYLT-GIQLAQGYLGRPDLTA 821
Cdd:PRK13388 306 REPGTPP------GS---IGRGA--PGVAIYNPeTLTECAVARfdahgallnadeaIGELVNTaGAGFFEGYYNNPEATA 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128569 822 SRFiadpfAPGerMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQAVTHA 889
Cdd:PRK13388 375 ERM-----RHG--MYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYA 435
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
475-886 |
5.77e-08 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 57.07 E-value: 5.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 475 ADARYLfSYREMREQVVALANLLRERGVKPGDSVAVALPRS---VFLTLA------LHAIVEAgaawlpldtGYPDDRLK 545
Cdd:PRK00174 94 GDSRKI-TYRELHREVCRFANALKSLGVKKGDRVAIYMPMIpeaAVAMLAcarigaVHSVVFG---------GFSAEALA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 546 MMLEDARPSLLITTDDQLPRFSDVP----------NLTSL---------CYNAPLTP---------QGSAPlqlsqPHHT 597
Cdd:PRK00174 164 DRIIDAGAKLVITADEGVRGGKPIPlkanvdealaNCPSVekvivvrrtGGDVDWVEgrdlwwhelVAGAS-----DECE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 598 A---------YIIFTSGSTGRPKGVmVGQTAivNRLLWMQnhypLTGEDVvaqktpcsFDVSVWEFFW------------ 656
Cdd:PRK00174 239 PepmdaedplFILYTSGSTGKPKGV-LHTTG--GYLVYAA----MTMKYV--------FDYKDGDVYWctadvgwvtghs 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 657 -----PFIAGAKLVMAE-----PEAHRdplaMQQFFAEYGVTTTHFVPSMLAAFVAsltpqtarqscatlkqvfcSGEAL 726
Cdd:PRK00174 304 yivygPLANGATTLMFEgvpnyPDPGR----FWEVIDKHKVTIFYTAPTAIRALMK-------------------EGDEH 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 727 PA--DLcrewQQL-----TGAPLHnlygPtEAAVdvsWYpafgeeLAQVRGSSVPIGYPVWNT---GLrildaMMHPVP- 795
Cdd:PRK00174 361 PKkyDL----SSLrllgsVGEPIN----P-EAWE---WY------YKVVGGERCPIVDTWWQTetgGI-----MITPLPg 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 796 -----PGVAGdLYLTGIQLA-------------QGYL--------------GRPDltasRFIADPFAPGERMYRTGDVAR 843
Cdd:PRK00174 418 atplkPGSAT-RPLPGIQPAvvdeegnpleggeGGNLvikdpwpgmmrtiyGDHE----RFVKTYFSTFKGMYFTGDGAR 492
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 16128569 844 WLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDV-EQAV 886
Cdd:PRK00174 493 RDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVaEAAV 536
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
453-868 |
5.88e-08 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 57.06 E-value: 5.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 453 PETTLSALVAEQAAKTPDAPALadaRYL------------FSYREMREQVVALANLLrERGVKPGDSVAVALPRSVFLTL 520
Cdd:PRK12476 32 PGTTLISLIERNIANVGDTVAY---RYLdhshsaagcaveLTWTQLGVRLRAVGARL-QQVAGPGDRVAILAPQGIDYVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 521 ALHAIVEAGAAWLPLDTgyPD-----DRLKMMLEDARPSLLITTD----------DQLPR--------FSDVPNLTSlcy 577
Cdd:PRK12476 108 GFFAAIKAGTIAVPLFA--PElpghaERLDTALRDAEPTVVLTTTaaaeavegflRNLPRlrrprviaIDAIPDSAG--- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 578 nAPLTPqgsAPLQLSQphhTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMqnhypLTGEDVVAQKT------PCSFDVSV 651
Cdd:PRK12476 183 -ESFVP---VELDTDD---VSHLQYTSGSTRPPVGVEITHRAVGTNLVQM-----ILSIDLLDRNThgvswlPLYHDMGL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 652 WEFFWPFIAGAKLVMAEPEAH-RDPL------------------------------------------------------ 676
Cdd:PRK12476 251 SMIGFPAVYGGHSTLMSPTAFvRRPQrwikalsegsrtgrvvtaapnfayewaaqrglpaegddidlsnvvliigsepvs 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 677 --AMQQF---FAEYGVTTTHFVPSMLAA----FVASLTPQtARQSCATL-KQVFCSGEA--LPADLCREWQQLT-GAPLH 743
Cdd:PRK12476 331 idAVTTFnkaFAPYGLPRTAFKPSYGIAeatlFVATIAPD-AEPSVVYLdREQLGAGRAvrVAADAPNAVAHVScGQVAR 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 744 NLYGpteAAVDvswyPAFGEELaqvrgssvpigypvwntglrildammhpvPPGVAGDLYLTGIQLAQGYLGRPDLTASR 823
Cdd:PRK12476 410 SQWA---VIVD----PDTGAEL-----------------------------PDGEVGEIWLHGDNIGRGYWGRPEETERT 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128569 824 FI------------ADPFAPGERMYRTGDVARWLDnGAVEYLGRSDDQLKIRG-----QRIE 868
Cdd:PRK12476 454 FGaklqsrlaegshADGAADDGTWLRTGDLGVYLD-GELYITGRIADLIVIDGrnhypQDIE 514
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
600-892 |
7.01e-08 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 55.77 E-value: 7.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 600 IIFTSGSTGRPKGVMVGQTAIVNR---LLWMQNhypLTGEDVVAQKTPCsFDVSVWEFFWP-FIAGAKLVMAepeAHRDP 675
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQALLAQalvLAVLQA---IDEGTVFLNSGPL-FHIGTLMFTLAtFHAGGTNVFV---RRVDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 676 LAMQQFFAEYGVTTTHFVPSMLAAFVASLTPQTARQSCatLKQVFCSGE---ALPADLCREWQQLTGaplhnlYGPTEAA 752
Cdd:cd17636 78 EEVLELIEAERCTHAFLLPPTIDQIVELNADGLYDLSS--LRSSPAAPEwndMATVDTSPWGRKPGG------YGQTEVM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 753 VDVSwYPAFGEELAQVRGSSVPIgypvwnTGLRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIAdpfapg 832
Cdd:cd17636 150 GLAT-FAALGGGAIGGAGRPSPL------VQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRG------ 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 833 eRMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPdveqAVTHACVI 892
Cdd:cd17636 217 -GWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHP----AVADAAVI 271
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
482-622 |
7.02e-08 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 56.84 E-value: 7.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 482 SYREMREQVVALANLLRERGVK--PGDSVAVALPRSVFLTLALHAIVEAGAAWLPL-DTGYPDDrLKMMLEDARPSLLIT 558
Cdd:cd05927 7 SYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPLyDTLGPEA-IEYILNHAEISIVFC 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128569 559 TDD-QLPRFSDVPNLTSLcYNAPLTPqgsaplqlSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVN 622
Cdd:cd05927 86 DAGvKVYSLEEFEKLGKK-NKVPPPP--------PKPEDLATICYTSGTTGNPKGVMLTHGNIVS 141
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
482-976 |
7.74e-08 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 56.71 E-value: 7.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 482 SYREMREQVVALANLLRER-GVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDD------------------ 542
Cdd:PRK05620 40 TFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDqivhiinhaedevivadp 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 543 ----RLKMMLED---ARPSLLITTDD-QLPRFSDVPNLTSLCYNAPLTPQGSAPLQLSQPHHT-AYIIFTSGSTGRPKGV 613
Cdd:PRK05620 120 rlaeQLGEILKEcpcVRAVVFIGPSDaDSAAAHMPEGIKVYSYEALLDGRSTVYDWPELDETTaAAICYSTGTTGAPKGV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 614 mvgqtAIVNRLLWMQNhYPLTGEDVVAQKTPCSFDVSV-------WEF-FWPFIAGAKLVMaePEAHRDPLAMQQFFAEY 685
Cdd:PRK05620 200 -----VYSHRSLYLQS-LSLRTTDSLAVTHGESFLCCVpiyhvlsWGVpLAAFMSGTPLVF--PGPDLSAPTLAKIIATA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 686 GVTTTHFVPSM-LAAFVASLTPQTARQScatLKQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAV--DVSWYPA-- 760
Cdd:PRK05620 272 MPRVAHGVPTLwIQLMVHYLKNPPERMS---LQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPvgTVARPPSgv 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 761 FGEELAQVRGSS----VPIGYPVWNTGlRILDAMMHPvppgvAGDLYLTGIQLAQGYL----GRPDLTASRFIADPFAPG 832
Cdd:PRK05620 349 SGEARWAYRVSQgrfpASLEYRIVNDG-QVMESTDRN-----EGEIQVRGNWVTASYYhsptEEGGGAASTFRGEDVEDA 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 833 ERMY------RTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPdveqAVTHACVINQAAATGGDaRQLV 906
Cdd:PRK05620 423 NDRFtadgwlRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAP----EVVECAVIGYPDDKWGE-RPLA 497
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128569 907 GYLVSQSGLPLDTSA--LQAQLRETLPPHMVPVVLLQLPQLPLSANGKLDRKAL-------PLPELKAQAPGRAPKAGS 976
Cdd:PRK05620 498 VTVLAPGIEPTRETAerLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLrqhladgDFEIIKLKGPGESGESDS 576
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
24-200 |
1.37e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 56.72 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 24 PSAWSVAHYVELTGEVDSPLLARAVVAGLAQADTLRMRFTEDNGEvWQWVDDALTfelPEIIDLRTNIDPHGTAQALMqA 103
Cdd:PRK05691 2809 PQHWNQALLLEPRQALDPALLEQALQALVEHHDALRLRFSQADGR-WQAEYRAVT---AQELLWQVTVADFAECAALF-A 2883
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 104 DLQQDLRVDSGkPLVFHQLIQVADNRWYWYQRYHHLLVDGFSFPAITRQIANIYCTWLRGEPTP-ASPFTPFADVVEEYQ 182
Cdd:PRK05691 2884 DAQRSLDLQQG-PLLRALLVDGPQGQQRLLLAIHHLVVDGVSWRVLLEDLQALYRQLSAGAEPAlPAKTSAFRDWAARLQ 2962
|
170
....*....|....*...
gi 16128569 183 QYRESEAWQRDAAFWAEQ 200
Cdd:PRK05691 2963 AYAGSESLREELGWWQAQ 2980
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
480-858 |
1.99e-07 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 55.51 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 480 LFSYREMREQVVALANLLRERGVKPGDSVAVA---LPRSVFLTLALHAIveaGAAWLPLDTGYPDDRLKMMLEDARPSLL 556
Cdd:cd17641 11 EFTWADYADRVRAFALGLLALGVGRGDVVAILgdnRPEWVWAELAAQAI---GALSLGIYQDSMAEEVAYLLNYTGARVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 557 ITTDDQ-----LPRFSDVPNLTSLCYNAP----------------LTPQGSAP-----------LQLSQPHHTAYIIFTS 604
Cdd:cd17641 88 IAEDEEqvdklLEIADRIPSVRYVIYCDPrgmrkyddprlisfedVVALGRALdrrdpglyereVAAGKGEDVAVLCTTS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 605 GSTGRPKGVMVGQTAIVNRLL------------WMQNHYPL--TGEDV--VAQKTPCSFDVSVWE--------------- 653
Cdd:cd17641 168 GTTGKPKLAMLSHGNFLGHCAaylaadplgpgdEYVSVLPLpwIGEQMysVGQALVCGFIVNFPEepetmmedlreigpt 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 654 -FFWP---FIAGAKLVMAEPEahrDPLAMQQFFAEYGV--------TTTHFVPSMLAAFVAS-------LTPQTARQSCA 714
Cdd:cd17641 248 fVLLPprvWEGIAADVRARMM---DATPFKRFMFELGMklglraldRGKRGRPVSLWLRLASwladallFRPLRDRLGFS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 715 TLKQVFCSGEALPADLCREWQQLtGAPLHNLYGPTEAAVDVSWYPAfgeelAQVRGSSVpiGYPVWNTGLRILDammhpv 794
Cdd:cd17641 325 RLRSAATGGAALGPDTFRFFHAI-GVPLKQLYGQTELAGAYTVHRD-----GDVDPDTV--GVPFPGTEVRIDE------ 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128569 795 ppgvAGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermYRTGDVARWLDNGAVEYLGRSDD 858
Cdd:cd17641 391 ----VGEILVRSPGVFVGYYKNPEATAEDFDEDGW------LHTGDAGYFKENGHLVVIDRAKD 444
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
481-885 |
5.22e-07 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 54.13 E-value: 5.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 481 FSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITT- 559
Cdd:PLN02654 121 LTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVITCn 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 560 ---------------DDQLPRFSDVPNLTSLCYN-------------------------APLTPQgSAPLQLSQPHHTAY 599
Cdd:PLN02654 201 avkrgpktinlkdivDAALDESAKNGVSVGICLTyenqlamkredtkwqegrdvwwqdvVPNYPT-KCEVEWVDAEDPLF 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 600 IIFTSGSTGRPKGVMvgqtaivnrllwmqnHypLTGEDVVAQKTPC--SFDVSVWEFFW-----------------PFIA 660
Cdd:PLN02654 280 LLYTSGSTGKPKGVL---------------H--TTGGYMVYTATTFkyAFDYKPTDVYWctadcgwitghsyvtygPMLN 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 661 GAKLVMAE-PEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPQTARQSCATLKQVFCSGEALPADLCREWQQLTG 739
Cdd:PLN02654 343 GATVLVFEgAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVG 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 740 ---APLHNLYGPTEAA------VDVSW--------YPAFGEELAQVRGSSVPI-----GYpvwntglrildAMMHPVPPG 797
Cdd:PLN02654 423 dsrCPISDTWWQTETGgfmitpLPGAWpqkpgsatFPFFGVQPVIVDEKGKEIegecsGY-----------LCVKKSWPG 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 798 VAGDLYltgiqlaqgylGRPDltasRFIADPFAPGERMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQ 877
Cdd:PLN02654 492 AFRTLY-----------GDHE----RYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALV 556
|
....*...
gi 16128569 878 ALPDVEQA 885
Cdd:PLN02654 557 SHPQCAEA 564
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
481-934 |
8.89e-07 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 53.24 E-value: 8.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 481 FSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLdtgYPD---DRLKMMLEDARPSLLI 557
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPL---YPTlnpDTIRYVLEHSESKALF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 558 T--TDDQLPRFSDVPNLTSLCYNAPLTP-----------QGSAPLQ---LSQPHHTAYIIFTSGSTGRPKGVMVGQTAIV 621
Cdd:cd05932 84 VgkLDDWKAMAPGVPEGLISISLPPPSAancqyqwddliAQHPPLEerpTRFPEQLATLIYTSGTTGQPKGVMLTFGSFA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 622 NRLLWMQNHYPLTGEDVVAQKTP-CSFDVSVWEFFWPFIAGAKLVMAEP--------EAHRDPLamqqFFAeygvttthf 692
Cdd:cd05932 164 WAAQAGIEHIGTEENDRMLSYLPlAHVTERVFVEGGSLYGGVLVAFAESldtfvedvQRARPTL----FFS--------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 693 VPSMLAAF---VASLTPQTARQscATLKQVFCSG-------EALPADLCRewQQLTGAplhnlyGPTEAAVdVSWYPAFG 762
Cdd:cd05932 231 VPRLWTKFqqgVQDKIPQQKLN--LLLKIPVVNSlvkrkvlKGLGLDQCR--LAGCGS------APVPPAL-LEWYRSLG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 763 EELAQVRGSSVPIGYPVWNTGLRILDAMMHPVPPGVA------GDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermY 836
Cdd:cd05932 300 LNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEvrisedGEILVRSPALMMGYYKDPEATAEAFTADGF------L 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 837 RTGDVARWLDNGAVEYLGRSDDQLKI-RGQRIELGEIDRVMQALPDVEQavthACVInqaaatGGDARQLVGYLV-SQSG 914
Cdd:cd05932 374 RTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEM----VCVI------GSGLPAPLALVVlSEEA 443
|
490 500
....*....|....*....|
gi 16128569 915 LPLDTSALQAQLRETLPPHM 934
Cdd:cd05932 444 RLRADAFARAELEASLRAHL 463
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
6-200 |
1.01e-06 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380472 [Multi-domain] Cd Length: 430 Bit Score: 52.70 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 6 PLVAAQPGIWMAEKLSELPSAWSVAHYVELTGEVDSPLLARAVVAGLAQADTLRMRFTEDNGEVWQWVDDA--LTFELPE 83
Cdd:cd20484 3 PLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIEPSkpLSFQEED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 84 IIDLR-TNIDPHGTAQALMQADLQQDlrvdsgkPLVFHQLIQVADNRWYWYQRYHHLLVDGFSFPAITRQIANIYCTWLR 162
Cdd:cd20484 83 ISSLKeSEIIAYLREKAKEPFVLENG-------PLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQ 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 16128569 163 G-EPTPASPFTPFADVVEEYQQYRESEAWQRDAAFWAEQ 200
Cdd:cd20484 156 GkQPTLASSPASYYDFVAWEQDMLAGAEGEEHRAYWKQQ 194
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
32-200 |
1.19e-06 |
|
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380458 [Multi-domain] Cd Length: 423 Bit Score: 52.49 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 32 YVELTGE-VDSPLLARAVVAGLAQADTLRMRFTEDnGEvwQWVDDALTFELPEIIDLRtNIDPHGTAQALMQ--ADL-QQ 107
Cdd:cd19535 29 YLEFDGEdLDPDRLERAWNKLIARHPMLRAVFLDD-GT--QQILPEVPWYGITVHDLR-GLSEEEAEAALEElrERLsHR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 108 DLRVDSGKplVFH-QLIQVADNRwywyQRYH----HLLVDGFSFPAITRQIANIYCTwlRGEPTPASPFTpFADVVEEYQ 182
Cdd:cd19535 105 VLDVERGP--LFDiRLSLLPEGR----TRLHlsidLLVADALSLQILLRELAALYED--PGEPLPPLELS-FRDYLLAEQ 175
|
170
....*....|....*...
gi 16128569 183 QYRESeAWQRDAAFWAEQ 200
Cdd:cd19535 176 ALRET-AYERARAYWQER 192
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
977-1045 |
1.21e-06 |
|
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 47.54 E-value: 1.21e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128569 977 ETIIAAAFSSLLGCDVQ--DADADFFA-LGGHSLLAMKLAAQLSRQVARQVTPGQVMVASTVAKLATIIDAE 1045
Cdd:COG0236 7 EERLAEIIAEVLGVDPEeiTPDDSFFEdLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEK 78
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
456-864 |
3.01e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 51.48 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 456 TLSALVAEQAAKTPDAPAL---------ADARYLFSYREMREQVVALANLLRERGVkPGDSVAVALPRSVFLTLALHAIV 526
Cdd:PRK05850 2 SVPSLLRERASLQPDDAAFtfidyeqdpAGVAETLTWSQLYRRTLNVAEELRRHGS-TGDRAVILAPQGLEYIVAFLGAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 527 EAGAAWLPLDT---GYPDDRLKMMLEDARPSLLITT----DD-----QLPRFSDVPNLTSLCYNAPLTPQGSAPLQLSQP 594
Cdd:PRK05850 81 QAGLIAVPLSVpqgGAHDERVSAVLRDTSPSVVLTTsavvDDvteyvAPQPGQSAPPVIEVDLLDLDSPRGSDARPRDLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 595 HhTAYIIFTSGSTGRPKGVMVG-QTAIVNRLLWMQNHYPLTGEDVVAQKTPCSfdvsvWEFFW-----------PFIAGA 662
Cdd:PRK05850 161 S-TAYLQYTSGSTRTPAGVMVShRNVIANFEQLMSDYFGDTGGVPPPDTTVVS-----WLPFYhdmglvlgvcaPILGGC 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 663 KLVMAEPEAH-RDPLAMQQFFAEYGvttthfvPSMLAA--FVASLTpqTARQSCATLK-------QVFCSG-EAL-PADL 730
Cdd:PRK05850 235 PAVLTSPVAFlQRPARWMQLLASNP-------HAFSAApnFAFELA--VRKTSDDDMAgldlggvLGIISGsERVhPATL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 731 CREWQQLtgAPLhNL--------YGPTEAAVDVSwYPAFGEELAQVR--------GSSVP---------IGYPV-WNTGL 784
Cdd:PRK05850 306 KRFADRF--APF-NLretairpsYGLAEATVYVA-TREPGQPPESVRfdyeklsaGHAKRcetgggtplVSYGSpRSPTV 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 785 RILDA-MMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRF---IADPFA--PGERMYRTGDVArWLDNGAVEYLGRSDD 858
Cdd:PRK05850 382 RIVDPdTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFgatLVDPSPgtPEGPWLRTGDLG-FISEGELFIVGRIKD 460
|
....*.
gi 16128569 859 QLKIRG 864
Cdd:PRK05850 461 LLIVDG 466
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
832-965 |
3.12e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 51.19 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 832 GERMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQAVthacVINQAAATGGdarQLVGYLVS 911
Cdd:PRK08308 289 GDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAV----VYRGKDPVAG---ERVKAKVI 361
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 16128569 912 QSGlPLDTSALQAQLRETLPPHMVPVVLLQLPQLPLSANGKLDRKALPLPELKA 965
Cdd:PRK08308 362 SHE-EIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLELGEVTA 414
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
1064-1165 |
3.59e-06 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440361 [Multi-domain] Cd Length: 221 Bit Score: 49.61 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 1064 NGPTLFCFHPASGFAWQFSVLSRYLDPQWSIIGI------QSPRPNGPMQTAANLDevceaHLATLLEQQPHGPYYLLGY 1137
Cdd:COG0596 22 DGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPdlrghgRSDKPAGGYTLDDLAD-----DLAALLDALGLERVVLVGH 96
|
90 100
....*....|....*....|....*...
gi 16128569 1138 SLGGTLAQGIAARlraRGEQVAFLGLLD 1165
Cdd:COG0596 97 SMGGMVALELAAR---HPERVAGLVLVD 121
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
503-627 |
1.38e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 49.34 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 503 KPGDSVAVALPRSVFLTLALHAIVEAGAAWLPL-DTGYPD--DRLKMMLEDARPSLLITTDD---------------QLP 564
Cdd:PRK07769 77 KPGDRVAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPGhvGRLHAVLDDCTPSAILTTTDsaegvrkffrarpakERP 156
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128569 565 RF---SDVPNLTSLCYNAPltpqgsaplqlsQPHH--TAYIIFTSGSTGRPKGVMVGQTAIVNRLLWM 627
Cdd:PRK07769 157 RViavDAVPDEVGATWVPP------------EANEdtIAYLQYTSGSTRIPAGVQITHLNLPTNVLQV 212
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
4-192 |
3.44e-05 |
|
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380461 [Multi-domain] Cd Length: 432 Bit Score: 48.03 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 4 HLPLVAAQPGIWMAEKLSELPSAWSVAHYVELTGEVDSPLLARAVVAGLAQADTLRMRFTEDNGEVWQWVDDALTFELPE 83
Cdd:cd19538 1 EIPLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYQLILEEDEATPKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 84 IIdlrTNIDPHGTAQALMQA-----DLQQDLRVDSgkplvfhQLIQVADNRWYWYQRYHHLLVDGFSFPAITRQIANIYC 158
Cdd:cd19538 81 EI---KEVDEEELESEINEAvrypfDLSEEPPFRA-------TLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYR 150
|
170 180 190
....*....|....*....|....*....|....
gi 16128569 159 TWLRGEPTPASPFTpfadvveeyQQYRESEAWQR 192
Cdd:cd19538 151 ARCKGEAPELAPLP---------VQYADYALWQQ 175
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
602-885 |
3.63e-05 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 47.82 E-value: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 602 FTSGSTGRPKGVM------VGQTAIVNrllwMQNHYPLTGEDVVAQKTPCsFDVSVW--EFFWPFIaGAKLVMaePEAHR 673
Cdd:PRK06018 184 YTSGTTGDPKGVLyshrsnVLHALMAN----NGDALGTSAADTMLPVVPL-FHANSWgiAFSAPSM-GTKLVM--PGAKL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 674 DPLAMQQFFAEYGVTTTHFVPS---MLAAFVasltpQTARQSCATLKQVFCSGEALPADLCREWQQLTGAPLHnLYGPTE 750
Cdd:PRK06018 256 DGASVYELLDTEKVTFTAGVPTvwlMLLQYM-----EKEGLKLPHLKMVVCGGSAMPRSMIKAFEDMGVEVRH-AWGMTE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 751 -------AAVDVSWYPAFGEELAQVRGSSvpiGYPVWNTGLRILDAMMHPVP-PGVA-GDLYLTGIQLAQGYLGrpdLTA 821
Cdd:PRK06018 330 msplgtlAALKPPFSKLPGDARLDVLQKQ---GYPPFGVEMKITDDAGKELPwDGKTfGRLKVRGPAVAAAYYR---VDG 403
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128569 822 SRFIADPFapgermYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQA 885
Cdd:PRK06018 404 EILDDDGF------FDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEA 461
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
602-885 |
5.97e-05 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 47.15 E-value: 5.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 602 FTSGSTGRPKGVMVGQ-----TAIVNRLLWMQNhypltgEDVVAQKTPCSFDVSVWEFFWPFIA--GAKLVMAEPEAHrd 674
Cdd:PLN02479 202 YTSGTTASPKGVVLHHrgaylMALSNALIWGMN------EGAVYLWTLPMFHCNGWCFTWTLAAlcGTNICLRQVTAK-- 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 675 plAMQQFFAEYGVttTHF--VPSMLAAFVASLTPQTARQSCATLkQVFCSGEALPADLCREWQQLtGAPLHNLYGPTEA- 751
Cdd:PLN02479 274 --AIYSAIANYGV--THFcaAPVVLNTIVNAPKSETILPLPRVV-HVMTAGAAPPPSVLFAMSEK-GFRVTHTYGLSETy 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 752 --AVDVSWYPAFgEELAQVRGSSVPIGYPVWNTGLRILDAM----MHPVPP--GVAGDLYLTGIQLAQGYLGRPDLTasr 823
Cdd:PLN02479 348 gpSTVCAWKPEW-DSLPPEEQARLNARQGVRYIGLEGLDVVdtktMKPVPAdgKTMGEIVMRGNMVMKGYLKNPKAN--- 423
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128569 824 fiADPFAPGerMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQA 885
Cdd:PLN02479 424 --EEAFANG--WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEA 481
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
716-882 |
1.16e-04 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 46.30 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 716 LKQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVDVswypaFGEELAQvrgssvpigypvwnTGLR---------I 786
Cdd:COG1541 205 LKKGIFGGEPWSEEMRKEIEERWGIKAYDIYGLTEVGPGV-----AYECEAQ--------------DGLHiwedhflveI 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 787 LD-AMMHPVPPGVAGDLYLTGiqlaqgyLGRpdltasrfiadpfapgERM----YRTGDVARWLD--------NGAVEY- 852
Cdd:COG1541 266 IDpETGEPVPEGEEGELVVTT-------LTK----------------EAMplirYRTGDLTRLLPepcpcgrtHPRIGRi 322
|
170 180 190
....*....|....*....|....*....|
gi 16128569 853 LGRSDDQLKIRGQRIELGEIDRVMQALPDV 882
Cdd:COG1541 323 LGRADDMLIIRGVNVFPSQIEEVLLRIPEV 352
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
77-421 |
1.31e-04 |
|
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380467 [Multi-domain] Cd Length: 395 Bit Score: 45.75 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 77 LTFELPEIID-----------------LRTNIDPHGTAQALmQA-------------DLQQDLRVDSGKPLVFHQ-LIQV 125
Cdd:cd19545 26 RVFELPPDIDlarlqaaweqvvqanpiLRTRIVQSDSGGLL-QVvvkespiswtestSLDEYLEEDRAAPMGLGGpLVRL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 126 ADNRWYWYQRY-----HHLLVDGFSFPAITRQIANIYctwlRGEPTPASPftPFADVVeEYQQYRESEAWQRdaaFWAE- 199
Cdd:cd19545 105 ALVEDPDTERYfvwtiHHALYDGWSLPLILRQVLAAY----QGEPVPQPP--PFSRFV-KYLRQLDDEAAAE---FWRSy 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 200 -QRRQLPPPASLSPAPLPGRSASADILRLKLEFTDgefRQLATqLSGVQRTdlalalaaLW---LGRLCNRMDYAAGFIF 275
Cdd:cd19545 175 lAGLDPAVFPPLPSSRYQPRPDATLEHSISLPSSA---SSGVT-LATVLRA--------AWalvLSRYTGSDDVVFGVTL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 276 MRRlgSAALTA----TGPVLNVLPLGIHIAAQETLPELATRLAAQLKKMRRHQRYDAEQIvRDSGRAAGDEPLFGPVLNI 351
Cdd:cd19545 243 SGR--NAPVPGieqiVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMIPFEHTGLQNI-RRLGPDARAACNFQTLLVV 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128569 352 KvfdYQLDIPDVQAQTHTLATGPVNDLELALFPdvhgdLSIEILANKQ------RYDEPTLiqHAERLKMLIAQFA 421
Cdd:cd19545 320 Q---PALPSSTSESLELGIEEESEDLEDFSSYG-----LTLECQLSGSglrvraRYDSSVI--SEEQVERLLDQFE 385
|
|
| PRK11126 |
PRK11126 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional |
1108-1152 |
1.70e-04 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
Pssm-ID: 236855 [Multi-domain] Cd Length: 242 Bit Score: 44.83 E-value: 1.70e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 16128569 1108 TAANLDEVCEaHLATLLEQQPHGPYYLLGYSLGGTLA-----QGIAARLR 1152
Cdd:PRK11126 45 SVDGFADVSR-LLSQTLQSYNILPYWLVGYSLGGRIAmyyacQGLAGGLC 93
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
482-889 |
2.44e-04 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 45.28 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 482 SYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGaawLPLDTGYP---DDRLKMMLEDARPSLLIT 558
Cdd:cd17639 7 SYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---IPIVTVYAtlgEDALIHSLNETECSAIFT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 559 TddqlPRFSDVpnltslcynapltpqgsaplqlsqphhtAYIIFTSGSTGRPKGVMV----------GQTAIVNRLLWMQ 628
Cdd:cd17639 84 D----GKPDDL----------------------------ACIMYTSGSTGNPKGVMLthgnlvagiaGLGDRVPELLGPD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 629 NHY----PL------TGEDVV-----------------AQKTPCSFDVSVwefFWPFIAGA---------KLVMAEPEAh 672
Cdd:cd17639 132 DRYlaylPLahifelAAENVClyrggtigygsprtltdKSKRGCKGDLTE---FKPTLMVGvpaiwdtirKGVLAKLNP- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 673 RDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPQTARQscAT---LKQVFCSGEALPADlCREWQQLTGAPLHNLYGPT 749
Cdd:cd17639 208 MGGLKRTLFWTAYQSKLKALKEGPGTPLLDELVFKKVRA--ALggrLRYMLSGGAPLSAD-TQEFLNIVLCPVIQGYGLT 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 750 E----AAVDVSWYPAFGEelaqvrgssvpIGYPVWNTGLRILD---AMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTAS 822
Cdd:cd17639 285 EtcagGTVQDPGDLETGR-----------VGPPLPCCEIKLVDweeGGYSTDKPPPRGEILIRGPNVFKGYYKNPEKTKE 353
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128569 823 RFIADpfapgeRMYRTGDVARWLDNGAVEYLGRSDDQLKIR-GQRIELGEIDRVMQALPDVEQAVTHA 889
Cdd:cd17639 354 AFDGD------GWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLVNNICVYA 415
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
39-192 |
3.83e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 45.33 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 39 VDSPLLARAVVAGLAQADTLRMRFTEDNGEvWQwvddaltfelpEIIDLRTNIDPHGTAQALMQADL-------QQDLRV 111
Cdd:PRK12316 1133 LDPDRLGRALERLVAHHDALRLRFREEDGG-WQ-----------QAYAAPQAGEVLWQRQAASEEELlalceeaQRSLDL 1200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 112 DSGkPLVFHQLIQVADNRWYWYQRYHHLLVDGFSFPAITRQIANIYCTWLRGEPTPASPFTPFADVVEEYQQYR--ESEA 189
Cdd:PRK12316 1201 EQG-PLLRALLVDMADGSQRLLLVIHHLVVDGVSWRILLEDLQRAYADLDADLPARTSSYQAWARRLHEHAGARaeELDY 1279
|
...
gi 16128569 190 WQR 192
Cdd:PRK12316 1280 WQA 1282
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
550-621 |
9.83e-04 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 43.57 E-value: 9.83e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128569 550 DARPSLLITTDDQLPRFSDVPNLTSlcyNAPLTPQgsaplqLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIV 621
Cdd:PLN02387 214 DSDSSLSGSSNWTVSSFSEVEKLGK---ENPVDPD------LPSPNDIAVIMYTSGSTGLPKGVMMTHGNIV 276
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
1065-1154 |
9.95e-04 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 42.30 E-value: 9.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 1065 GPTLFCFHPASGFAWQFSVLSRYL-DPQWSIIGI------QSPRPNGPMQTAANLDEVCEAhLATLLEQQPHGPYYLLGY 1137
Cdd:COG2267 28 RGTVVLVHGLGEHSGRYAELAEALaAAGYAVLAFdlrghgRSDGPRGHVDSFDDYVDDLRA-ALDALRARPGLPVVLLGH 106
|
90
....*....|....*..
gi 16128569 1138 SLGGTLAQGIAARLRAR 1154
Cdd:COG2267 107 SMGGLIALLYAARYPDR 123
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
965-1045 |
1.01e-03 |
|
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.
Pssm-ID: 214834 [Multi-domain] Cd Length: 86 Bit Score: 39.54 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 965 AQAPGRAPKAGSETIIAAAFSSLLGC---DVQDADADFFALGGHSLLAMKLAAQLSRQVARQVTPGQVMVASTVAKLATI 1041
Cdd:smart00823 2 AALPPAERRRLLLDLVREQVAAVLGHaaaEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEH 81
|
....
gi 16128569 1042 IDAE 1045
Cdd:smart00823 82 LAAE 85
|
|
| beta-lac_NRPS |
cd19547 |
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ... |
6-203 |
1.17e-03 |
|
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.
Pssm-ID: 380469 [Multi-domain] Cd Length: 422 Bit Score: 43.07 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 6 PLVAAQPGIWMAEKLSELPSAWSVAHYVELTGEVDSPLLARAVVAGLAQADTLRMRFT-EDNGEVWQWVDDALtfELPEI 84
Cdd:cd19547 3 PLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTwRDRAEPLQYVRDDL--APPWA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 85 IDLRTNIDPHGTAQ---ALMQADLQQDLRVDSGkPLVFHQLIQVADNRWYWYQRYHHLLVDGFSFPAITRQIANIYCTWL 161
Cdd:cd19547 81 LLDWSGEDPDRRAElleRLLADDRAAGLSLADC-PLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16128569 162 RGEPTPASPFTPFADvveeYQQYRESEAWQRDAA--FWAEQRRQ 203
Cdd:cd19547 160 HGREPQLSPCRPYRD----YVRWIRARTAQSEESerFWREYLRD 199
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
596-873 |
3.09e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 41.65 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 596 HTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTGEDVVAQKTPCSFDVSVWEFFWPFIA-GAKLVMAEPEAHRD 674
Cdd:PTZ00237 255 HPLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHGFLYGSLSlGNTFVMFEGGIIKN 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 675 PLAMQQFFA---EYGVTTTHFVPSMLAAFVASLTPQTARQS---CATLKQVFCSGEALPADLCREWQQLTGAPLHNLYGP 748
Cdd:PTZ00237 335 KHIEDDLWNtieKHKVTHTLTLPKTIRYLIKTDPEATIIRSkydLSNLKEIWCGGEVIEESIPEYIENKLKIKSSRGYGQ 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 749 TEAAVdvSWYPAFGEELAQVRGSSVP-------------IGYPVWNTGLRildAMMHPVPPGVAGDLYLTGIQLAQGYlg 815
Cdd:PTZ00237 415 TEIGI--TYLYCYGHINIPYNATGVPsifikpsilsedgKELNVNEIGEV---AFKLPMPPSFATTFYKNDEKFKQLF-- 487
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 16128569 816 rpdltaSRFiadpfaPGerMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEID 873
Cdd:PTZ00237 488 ------SKF------PG--YYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIE 531
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
800-868 |
3.68e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 41.63 E-value: 3.68e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128569 800 GDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermYRTGDVARWLDNGAVEYLGRSDDQLKI-RGQRIE 868
Cdd:PTZ00342 542 GELLIKSDSIFSGYFLEKEQTKNAFTEDGY------FKTGDIVQINKNGSLTFLDRSKGLVKLsQGEYIE 605
|
|
| |
